CAZypedia - User contributions [en-ca]

Carbohydrate Binding Module Family 50

2014-06-24T00:02:57Z

Takayuki Ohnuma:

{{CuratorApproved}}
* [[Author]]: ^^^Takayuki Ohnuma^^^ and ^^^Toki Taira^^^
* [[Responsible Curator]]: ^^^Takayuki Ohnuma^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM50.html
|}
</div>


== Ligand specificities ==
CBM50 members are also known as LysM domains. They bind to the N-acetylglucosamine residues in bacterial peptidoglycans and in chitin. For example CBM50 of ''Lactococcus lactis'' ''N''-acetylglucosaminidase AcmA was shown to bind to the glycan chain of bacterial peptidoglycans, a β-1,4 linked heteropolymer of alternating ''N''-acetylglucosamine (GlcNAc) and ''N''-acetylmuramic acid (MurNAc) <cite>Steen2003</cite>. A CBM50 module from ''Pteris ryukyuensis'' chitinase-A (PrChi-A) was demonstrated to bind to chitin, a β-1,4-linked homopolymer of GlcNAc <cite>Onaga2008</cite>. From isothermal titration calorimetry, the CBM50 module from PrChi-A was found to bind to (GlcNAc)<sub>n</sub> (n=4,5) with the binding stoichiometry of 1:1, whereas no significant binding heat was observed for the binding to (GlcNAc)<sub>2</sub> <cite>Ohnuma2008</cite>. The binding site of the CBM50 module can accommodate at least three saccharide units.

== Structural Features ==
CBM50 modules are about 50 amino acids long. The three-dimensional structures of several CBM50 modules attached to carbohydrate-active enzymes have been deposited in the Protein Data Bank (example PDB entries: [{{PDBlink}}1e0g 1e0g] <cite>Bateman2000</cite>, [{{PDBlink}}2mkx 2mkx] and [{{PDBlink}}4pxv 4pxv]). The CBM50 modules have a βααβ fold with the two helices packing against one side of the two-stranded antiparallel β-sheet. Although no crystal structure of the CBM50 module in complex with the ligand has been determined yet, Ohnuma ''et al''. first identified the chitin oligosaccharide binding site of the CBM50 module from PrChi-A based on the NMR titration experiments <cite>Ohnuma2008</cite>. The chitin oligosaccharide binding site was estimated to be located in a shallow groove formed by the N-terminal part of helix 1, the loop between strand 1 and helix 1, the C-terminal part of helix 2, and the loop between helix 2 and strand 2.

== Functionalities ==
CBM50 modules are generally found in bacterial lysins including muramidase <cite>Chu1992</cite>, ''N''-acetylglucosaminidase <cite>Steen2003</cite>, γ-D-glutamate-meso-diaminopimelate muropeptidase <cite>Margot1999</cite> and ''N''-acetylmuramoyl-L-alanine amidase <cite>Kajimura2005</cite>. The CBM50 modules in lysins are shown to bind to bacterial peptidoglycan and involved in cell division by localizing these enzymes to the divisional site <cite>Visweswaran2013</cite>. CBM50 modules were also found in family GH18 chitinases <cite>Onaga2008 Gruger2011</cite>, and contribute to the antifungal activity of the enzymes through their binding ability to chitinous component of the fungal cell wall. CBM50 modules are found not only in carbohydrate-active enzymes but also in LysM-containing plant cell surface receptors for chitin oligosaccharides and their derivatives <cite>Kaku2006 Limpens2003</cite> and fungal effectors <cite>Bolton2008</cite>. The receptor proteins are involved in plant-microbe interactions upon symbiosis or infection.

== Family Firsts ==
;First Identified
CBM50s are also known as LysM domains. The LysM domain was first identified in lysozyme from ''Bacillus phage'' f29 <cite>Garvey1986</cite>. LysM domains were first classified as a CBM in 2008 after demonstrating chitin oligosaccharide binding by an ''N''-terminal LysM domain from ''Pteris ryukyuensis'' chitinase-A <cite>Ohnuma2008</cite>.
;First Structural Characterization
The first three-dimensional structure of CBM50 module was determined for the LysM domain from ''E. coli'' membrane-bond lytic murein transglycosylase D (MltD) (PDB entry: [{{PDBlink}}1e0g 1e0g]) by NMR spectroscopy <cite>Bateman2000</cite>.

== References ==
<biblio>
#Steen2003 pmid=12684515
#Onaga2008 pmid=18310304
#Ohnuma2008 pmid=18083709
#Bateman2000 pmid=10843862
#Chu1992 pmid=1347040
#Margot1999 pmid=10206711
#Kajimura2005 pmid=16262792
#Visweswaran2013 pmid=23951292
#Gruger2011 pmid=20843785
#Kaku2006 pmid=16829581
#Limpens2003 pmid=12947035
#Bolton2008 pmid=18452583
#Garvey1986 pmid=3027653
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM050]]

Carbohydrate Binding Module Family 50

2014-06-20T04:32:34Z

Takayuki Ohnuma:

{{UnderConstruction}}
* [[Author]]: ^^^Takayuki Ohnuma^^^ and ^^^Toki Taira^^^
* [[Responsible Curator]]: ^^^Takayuki Ohnuma^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM50.html
|}
</div>


== Ligand specificities ==
CBM50 members are also known as LysM domains. They bind to the N-acetylglucosamine residues in bacterial peptidoglycans and in chitin. For example CBM50 of ''Lactococcus lactis'' ''N''-acetylglucosaminidase AcmA was shown to bind to the glycan chain of bacterial peptidoglycans, a β-1,4 linked heteropolymer of alternating ''N''-acetylglucosamine (GlcNAc) and ''N''-acetylmuramic acid (MurNAc) <cite>Steen2003</cite>. A CBM50 module from ''Pteris ryukyuensis'' chitinase-A (PrChi-A) was demonstrated to bind to chitin, a β-1,4-linked homopolymer of GlcNAc <cite>Onaga2008</cite>. From isothermal titration calorimetry, the CBM50 module from PrChi-A was found to bind to (GlcNAc)<sub>n</sub> (n=4,5) with the binding stoichiometry of 1:1, whereas no significant binding heat was observed for the binding to (GlcNAc)<sub>2</sub> <cite>Ohnuma2008</cite>. The binding site of the CBM50 module can accommodate at least three saccharide units.

== Structural Features ==
CBM50 modules are about 50 amino acids long. The three-dimensional structures of several CBM50 modules attached to carbohydrate-active enzymes have been deposited in the Protein Data Bank (example PDB entries: [{{PDBlink}}1e0g 1e0g] <cite>Bateman2000</cite>, [{{PDBlink}}2mkx 2mkx] and [{{PDBlink}}4pxv 4pxv]). The CBM50 modules have a βααβ fold with the two helices packing against one side of the two-stranded antiparallel β-sheet. Although no crystal structure of the CBM50 module in complex with the ligand has been determined yet, Ohnuma ''et al''. first identified the chitin oligosaccharide binding site of the CBM50 module from PrChi-A based on the NMR titration experiments <cite>Ohnuma2008</cite>. The chitin oligosaccharide binding site was estimated to be located in a shallow groove formed by the N-terminal part of helix 1, the loop between strand 1 and helix 1, the C-terminal part of helix 2, and the loop between helix 2 and strand 2.

== Functionalities ==
CBM50 modules are generally found in bacterial lysins including muramidase <cite>Chu1992</cite>, ''N''-acetylglucosaminidase <cite>Steen2003</cite>, γ-D-glutamate-meso-diaminopimelate muropeptidase <cite>Margot1999</cite> and ''N''-acetylmuramoyl-L-alanine amidase <cite>Kajimura2005</cite>. The CBM50 modules in lysins are shown to bind to bacterial peptidoglycan and involved in cell division by localizing these enzymes to the divisional site <cite>Visweswaran2013</cite>. CBM50 modules were also found in family GH18 chitinases <cite>Onaga2008 Gruger2011</cite>, and contribute to the antifungal activity of the enzymes through their binding ability to chitinous component of the fungal cell wall. CBM50 modules are found not only in carbohydrate-active enzymes but also in LysM-containing plant cell surface receptors for chitin oligosaccharides and their derivatives <cite>Kaku2006 Limpens2003</cite> and fungal effectors <cite>Bolton2008</cite>. The receptor proteins are involved in plant-microbe interactions upon symbiosis or infection.

== Family Firsts ==
;First Identified
CBM50s are also known as LysM domains. The LysM domain was first identified in lysozyme from ''Bacillus phage'' f29 <cite>Garvey1986</cite>. LysM domains were first classified as a CBM in 2008 after demonstrating chitin oligosaccharide binding by an ''N''-terminal LysM domain from ''Pteris ryukyuensis'' chitinase-A <cite>Ohnuma2008</cite>.
;First Structural Characterization
The first three-dimensional structure of CBM50 module was determined for the LysM domain from ''E. coli'' membrane-bond lytic murein transglycosylase D (MltD) (PDB entry: [{{PDBlink}}1e0g 1e0g]) by NMR spectroscopy <cite>Bateman2000</cite>.

== References ==
<biblio>
#Steen2003 pmid=12684515
#Onaga2008 pmid=18310304
#Ohnuma2008 pmid=18083709
#Bateman2000 pmid=10843862
#Chu1992 pmid=1347040
#Margot1999 pmid=10206711
#Kajimura2005 pmid=16262792
#Visweswaran2013 pmid=23951292
#Gruger2011 pmid=20843785
#Kaku2006 pmid=16829581
#Limpens2003 pmid=12947035
#Bolton2008 pmid=18452583
#Garvey1986 pmid=3027653
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM050]]

Carbohydrate Binding Module Family 50

2014-05-30T01:24:44Z

Takayuki Ohnuma:

{{UnderConstruction}}
* [[Author]]: ^^^Takayuki Ohnuma^^^ and ^^^Toki Taira^^^
* [[Responsible Curator]]: ^^^Takayuki Ohnuma^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM50.html
|}
</div>


== Ligand specificities ==
A CBM50 module, also known as LysM domain, from ''Lactococcus lactis'' ''N''-acetylglucosaminidase AcmA was shown to bind to the glycan chain of bacterial peptidoglycans, a β-1,4 linked heteropolymer of alternating ''N''-acetylglucosamine (GlcNAc) and ''N''-acetylmuramic acid (MurNAc) <cite>Steen2003</cite>. A CBM50 module from ''Pteris ryukyuensis'' chitinase-A (PrChi-A) was demonstrated to bind to chitin, a β-1,4-linked homopolymer of GlcNAc <cite>Onaga2008</cite>. CBM50 modules appear to recognize the GlcNAc residue of these polysaccharides. From isothermal titration calorimetry, the CBM50 module from PrChi-A was found to bind to (GlcNAc)<sub>n</sub> (n=4,5) with the binding stoichiometry of 1:1, whereas no significant binding heat was observed for the binding to (GlcNAc)<sub>2</sub> <cite>Ohnuma2008</cite>. The binding site of the CBM50 module can accommodate at least three saccharide units.

== Structural Features ==
CBM50 modules are about 50 amino acids long. The three-dimensional structures of three CBM50 modules attached to carbohydrate-active enzymes have been deposited in the Protein Data Bank (PDB entries: 1E0G <cite>Bateman2000</cite>, 2MKX and 4PXV). The CBM50 modules have a βααβ fold with the two helices packing against one side of the two-stranded antiparallel β-sheet. Although no crystal structure of the CBM50 module in complex with the ligand has been determined yet, Ohnuma ''et al''. first identified the chitin oligosaccharide binding site of the CBM50 module from PrChi-A based on the NMR titration experiments <cite>Ohnuma2008</cite>. The chitin oligosaccharide binding site was estimated to be located in a shallow groove formed by the N-terminal part of helix 1, the loop between strand 1 and helix 1, the C-terminal part of helix 2, and the loop between helix 2 and strand 2.

== Functionalities ==
CBM50 modules are generally found in bacterial lysins including muramidase <cite>Chu1992</cite>, ''N''-acetylglucosaminidase <cite>Steen2003</cite>, γ-D-glutamate-meso-diaminopimelate muropeptidase <cite>Margot1999</cite> and ''N''-acetylmuramoyl-L-alanine amidase <cite>Kajimura2005</cite>. The CBM50 modules in lysins are shown to bind to bacterial peptidoglycan, and involved in cell division by localizing these enzymes to the divisional site <cite>Visweswaran2013</cite>. CBM50 modules were also found in family GH18 chitinases <cite>Onaga2008 Gruger2011</cite>, and contribute to the antifungal activity of the enzymes through their binding ability to chitinous component of the fungal cell wall. CBM50 modules are found not only in carbohydrate-active enzymes but also in LysM-containing plant cell surface receptors for chitin oligosaccharides and their derivatives <cite>Kaku2006 Limpens2003</cite> and fungal effectors <cite>Bolton2008</cite>. The receptor proteins are involved in plant-microbe interactions upon symbiosis or infection.

== Family Firsts ==
;First Identified
Family 50 CBMs have been known as LysM domains. LysM domain was first identified in the lysozyme from ''Bacillus phage'' f29 <cite>Garvey1986</cite>. LysM domain was first classified as a CBM in 2008 after demonstrating chitin oligosaccharide binding by an ''N''-terminal LysM domain from ''Pteris ryukyuensis'' chitinase-A <cite>Ohnuma2008</cite>.
;First Structural Characterization
The first three-dimensional structure of CBM50 module was determined for the LysM domain from ''E. coli'' membrane-bond lytic murein transglycosylase D (MltD) (PDB entry: 1E0G) by NMR spectroscopy <cite>Bateman2000</cite>.

== References ==
<biblio>
#Steen2003 pmid=12684515
#Onaga2008 pmid=18310304
#Ohnuma2008 pmid=18083709
#Bateman2000 pmid=10843862
#Chu1992 pmid=1347040
#Margot1999 pmid=10206711
#Kajimura2005 pmid=16262792
#Visweswaran2013 pmid=23951292
#Gruger2011 pmid=20843785
#Kaku2006 pmid=16829581
#Limpens2003 pmid=12947035
#Bolton2008 pmid=18452583
#Garvey1986 pmid=3027653
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM050]]

Carbohydrate Binding Module Family 50

2014-05-29T12:05:56Z

Takayuki Ohnuma:

{{UnderConstruction}}
* [[Author]]: ^^^Takayuki Ohnuma^^^ and ^^^Toki Taira^^^
* [[Responsible Curator]]: ^^^Takayuki Ohnuma^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM50.html
|}
</div>


== Ligand specificities ==
A CBM50 module, also known as LysM domain, from ''Lactococcus lactis'' ''N''-acetylglucosaminidase AcmA was shown to bind to the glycan chain of bacterial peptidoglycans, a β-1,4 linked heteropolymer of alternating ''N''-acetylglucosamine (GlcNAc) and ''N''-acetylmuramic acid (MurNAc) <cite>Steen2003</cite>. A CBM50 module from ''Pteris ryukyuensis'' chitinase-A (PrChi-A) was demonstrated to bind to chitin, a β-1,4-linked homopolymer of GlcNAc <cite>Onaga2008</cite>. CBM50 modules appear to recognize the GlcNAc residue of these polysaccharides. From isothermal titration calorimetry, the CBM50 module from PrChi-A was found to bind to (GlcNAc)<sub>n</sub> (n=4,5) with the binding stoichiometry of 1:1, whereas no significant binding heat was observed for the binding to (GlcNAc)<sub>2</sub> <cite>Ohnuma2008</cite>. The binding site of the CBM50 module can accommodate at least three saccharide units.

== Structural Features ==
CBM50 modules are about 50 amino acids long. The three-dimensional structures of three CBM50 modules attached to carbohydrate-active enzymes have been deposited in the Protein Data Bank (PDB entries: 1E0G <cite>Bateman2000</cite>, 2MKX and 4PXV). The CBM50 modules have a βααβ fold with the two helices packing against one side of the two-stranded antiparallel β-sheet. Although no crystal structure of the CBM50 module in complex with the ligand has been determined yet, Ohnuma et al. first identified the chitin oligosaccharide binding site of the CBM50 module from PrChi-A based on the NMR titration experiments <cite>Ohnuma2008</cite>. The chitin oligosaccharide binding site was estimated to be located in a shallow groove formed by the N-terminal part of helix 1, the loop between strand 1 and helix 1, the C-terminal part of helix 2, and the loop between helix 2 and strand 2.

== Functionalities ==
CBM50 modules are generally found in bacterial lysins including muramidase <cite>Chu1992</cite>, ''N''-acetylglucosaminidase <cite>Steen2003</cite>, γ-D-glutamate-meso-diaminopimelate muropeptidase <cite>Margot1999</cite> and ''N''-acetylmuramoyl-L-alanine amidase <cite>Kajimura2005</cite>. The CBM50 modules in lysins are shown to bind to bacterial peptidoglycan, and involved in cell division by localizing these enzymes to the divisional site <cite>Visweswaran2013</cite>. CBM50 modules were also found in family GH18 chitinases <cite>Onaga2008 Gruger2011</cite>, and contribute to the antifungal activity of the enzymes through their binding ability to chitinous component of the fungal cell wall. CBM50 modules are found not only in carbohydrate-active enzymes but also in LysM-containing plant cell surface receptors for chitin oligosaccharides and their derivatives <cite>Kaku2006 Limpens2003</cite> and fungal effectors <cite>Bolton2008</cite>. The receptor proteins are involved in plant-microbe interactions upon symbiosis and or infection.

== Family Firsts ==
;First Identified
Family 50 CBMs have been known as LysM domains. LysM domain was first identified in the lysozyme from ''Bacillus phage'' f29 <cite>Garvey1986</cite>. LysM domain was first classified as a CBM in 2008 after demonstrating chitin oligosaccharide binding by an ''N''-terminal LysM domain from ''Pteris ryukyuensis'' chitinase-A Ohnuma2008.
;First Structural Characterization
The first three-dimensional structure of CBM50 module was determined for the LysM domain from ''E. coli'' membrane-bond lytic murein transglycosylase D (MltD) (PDB entry: 1E0G) by NMR spectroscopy <cite>Bateman2000</cite>.

== References ==
<biblio>
#Steen2003 pmid=12684515
#Onaga2008 pmid=18310304
#Ohnuma2008 pmid=18083709
#Bateman2000 pmid=10843862
#Chu1992 pmid=1347040
#Margot1999 pmid=10206711
#Kajimura2005 pmid=16262792
#Visweswaran2013 pmid=23951292
#Gruger2011 pmid=20843785
#Kaku2006 pmid=16829581
#Limpens2003 pmid=12947035
#Bolton2008 pmid=18452583
#Garvey1986 pmid=3027653
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM050]]

Carbohydrate Binding Module Family 50

2014-05-29T11:24:43Z

Takayuki Ohnuma:

{{UnderConstruction}}
* [[Author]]: ^^^Takayuki Ohnuma^^^ and ^^^Toki Taira^^^
* [[Responsible Curator]]: ^^^Takayuki Ohnuma^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM50.html
|}
</div>


== Ligand specificities ==
A CBM50 module, also known as LysM domain, from Lactococcus lactis N-acetylglucosaminidase AcmA was shown to bind to the glycan chain of bacterial peptidoglycans, a -1,4 linked heteropolymer of alternating N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid (MurNAc) [1]. A CBM50 module from Pteris ryukyuensis chitinase-A (PrChi-A) was demonstrated to bind to chitin, a -1,4-linked homopolymer of GlcNAc [2]. CBM50 modules appear to recognize the GlcNAc residue of these polysaccharides. From isothermal titration calorimetry, the CBM50 module from PrChi-A was found to bind to (GlcNAc)n (n=4,5) with the binding stoichiometry of 1:1, whereas no significant binding heat was observed for the binding to (GlcNAc)2 [3]. The binding site of the CBM50 module can accommodate at least three saccharide units.

== Structural Features ==
CBM50 modules are about 50 amino acids long. The three-dimensional structures of three CBM50 modules attached to carbohydrate-active enzymes have been deposited in the Protein Data Bank (PDB entries: 1E0G [4], 2MKX and 4PXV). The CBM50 modules have a βααβ fold with the two helices packing against one side of the two-stranded antiparallel β-sheet. Although no crystal structure of the CBM50 module in complex with the ligand has been determined yet, Ohnuma et al. first identified the chitin oligosaccharide binding site of the CBM50 module from PrChi-A based on the NMR titration experiments [3]. The chitin oligosaccharide binding site was estimated to be located in a shallow groove formed by the N-terminal part of helix 1, the loop between strand 1 and helix 1, the C-terminal part of helix 2, and the loop between helix 2 and strand 2.

== Functionalities ==
CBM50 modules are generally found in bacterial lysins including muramidase [5], N-acetylglucosaminidase [1], -D-glutamate-meso-diaminopimelate muropeptidase [6] and N-acetylmuramoyl-L-alanine amidase [7]. The CBM50 modules in lysins are shown to bind to bacterial peptidoglycan, and involved in cell division by localizing these enzymes to the divisional site [9]. CBM50 modules were also found in family GH18 chitinases [2,8], and contribute to the antifungal activity of the enzymes through their binding ability to chitinous component of the fungal cell wall. CBM50 modules are found not only in carbohydrate-active enzymes but also in LysM-containing plant cell surface receptors for chitin oligosaccharides and their derivatives [10,11] and fungal effectors [12]. The receptor proteins are involved in plant-microbe interactions upon symbiosis and or infection.

== Family Firsts ==
;First Identified
Family 50 CBMs have been known as LysM domains. LysM domain was first identified in the lysozyme from Bacillus phage f29 [13]. LysM domain was first classified as a CBM in 2008 after demonstrating chitin oligosaccharide binding by an N-terminal LysM domain from Pteris ryukyuensis chitinase-A [2,3].
;First Structural Characterization
The first three-dimensional structure of CBM50 module was determined for the LysM domain from E. coli membrane-bond lytic murein transglycosylase D (MltD) (PDB entry: 1E0G) by NMR spectroscopy [4].

== References ==
<biblio>
#Steen2003 pmid=12684515
#Onaga2008 pmid=18310304
#Ohnuma2008 pmid=18083709
#Bateman2000 pmid=10843862
#Chu1992 pmid=1347040
#Margot1999 pmid=10206711
#Kajimura2005 pmid=16262792
#Gruger2011 pmid=20843785
#Visweswaran2013 pmid=23951292
#Kaku2006 pmid=16829581
#Limpens2003 pmid=12947035
#Bolton2008 pmid=18452583
#Garvey1986 pmid=3027653
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM050]]

User:Takayuki Ohnuma

2014-05-26T02:13:32Z

Takayuki Ohnuma:

User:Takayuki Ohnuma

2014-05-22T09:16:12Z

Takayuki Ohnuma:

[[File:Taka.jpg|right|150px|caption]]Takayuki Ohnuma is an assistant professor at Department of Advanced Bioscience, Faculty of Agriculture, Kinki University located in Nara, Japan.
He received PhD degree in 2002 from Graduate School of Agriculture in Kyushu University. His research program currently focuses on the structures and functions of plant chitinases (GH18 and GH19), including their CBMs (CBM18 and CBM50), which are involved in plant self-defense against fungal pathogens [1-11]. In 2013, He and his colabolater published [2] the structure of a complex of rye family 19 chitinase with two molecules of (GlcNAc)<sub>4</sub>. This is the first report on the complete subsite mapping of GH19 chitinase.

----

References

# Ohnuma T, Umemoto N, Nagata T, Shinya S, Numata T, Taira T, Fukamizo T. Crystal structure of a "loopless" GH19 chitinase in complex with chitin tetrasaccharide spanning the catalytic center. ''Biochim Biophys Acta'', 1844, 793-802 (2014)
# Ohnuma T, Umemoto N, Kondo K, Numata T, Fukamizo T. Complete subsite mapping of a "loopful" GH19 chitinase from rye seeds based on its crystal structure. ''FEBS Lett'', 587, 2691-7 (2013)
# Ohnuma T, Taira T, Fukamizo T. Antifungal activity of recombinant class V chitinases from ''Nicotiana tabacum'' and ''Arabidopsis thaliana''. ''J Appl Glycosci'', 59, 1, 47-50 (2012)
# Umemoto N, Ohnuma T, Mizuhara M, Sato H, Skriver K, Fukamizo T. Introduction of a tryptophan side chain into subsite +1 enhances transglycosylation activity of a GH-18 chitinase from ''Arabidopsis thaliana'', AtChiC. ''Glycobiology'', 23, 81-90 (2013)
# Ohnuma T, Numata T, Osawa T, Inanaga H, Okazaki Y, Shinya S, Kondo K, Fukuda T, Fukamizo T. Crystal structure and chitin oligosaccharide-binding mode of a 'loopful' family GH19 chitinase from rye, ''Secale cereale'', seeds. ''FEBS J'', 19, 3639-3651 (2012)
# Umemoto N, Ohnuma T, Urpilainen H, Yamamoto T, Numata T, Fukamizo T. Role of tryptophan residues in a class V chitinase from ''Nicotiana tabacum''. ''Biosci Biotechnol Biochem'', 76,778-784 (2012)
# Ohnuma T, Fukuda T, Dozen S, Honda Y, Kitaoka M, Fukamizo T. A glycosynthase derived from an inverting GH19 chitinase from the moss ''Bryum coronatum''. ''Biochem J'', 444, 437-443 (2012)
# Shinya S, Ohnuma T, Kawamura S, Torikata T, Nishimura S, Katoh E, Fukamizo T. Interaction of a goose-type lysozyme with chitin oligosaccharides as determined by NMR spectroscopy. ''J Biochem'', 150, 569-577 (2011)
# Ohnuma T, Sørlie M, Fukuda T, Kawamoto N, Taira T, Fukamizo T. Chitin oligosaccharide binding to a family GH19 chitinase from the moss ''Bryum coronatum''. ''FEBS J'', 278, 3991-4001 (2011)
# Ohnuma T, Numata T, Osawa T, Mizuhara M, Lampela O, Juffer AH, Skriver K, Fukamizo T. A class V chitinase from ''Arabidopsis thaliana'': gene responses, enzymatic properties, and crystallographic analysis. ''Planta'', 234, 123-137 (2011)
# Ohnuma T, Numata T, Osawa T, Mizuhara M, Vårum KM, Fukamizo T. Crystal structure and mode of action of a class V chitinase from ''Nicotiana tabacum''. ''Plant Mol Biol'', 75, 291-304 (2011)
[[Category:Contributors|Ohnuma, Takayuki]]

User:Takayuki Ohnuma

2014-05-22T09:12:41Z

Takayuki Ohnuma:

[[File:Taka.jpg|right|150px|caption]]Takayuki Ohnuma is an assistant professor at Department of Advanced Bioscience, Faculty of Agriculture, Kinki University located in Nara, Japan.
He received PhD degree in 2002 from Graduate School of Agriculture in Kyushu University. His research program currently focuses on the structures and functions of plant chitinases (GH18 and GH19), including their CBMs (CBM18 and CBM50), which are involved in plant self-defense against fungal pathogens. In 2013, He and his colabolater published [9] the structure of a complex of rye family 19 chitinase with two molecules of (GlcNAc)4. This is the first report on the complete subsite mapping of GH19 chitinase.

----

References

# Ohnuma T, Umemoto N, Nagata T, Shinya S, Numata T, Taira T, Fukamizo T. Crystal structure of a "loopless" GH19 chitinase in complex with chitin tetrasaccharide spanning the catalytic center. ''Biochim Biophys Acta'', 1844, 793-802 (2014)
# Ohnuma T, Umemoto N, Kondo K, Numata T, Fukamizo T. Complete subsite mapping of a "loopful" GH19 chitinase from rye seeds based on its crystal structure. ''FEBS Lett'', 587, 2691-7 (2013)
# Ohnuma T, Taira T, Fukamizo T. Antifungal activity of recombinant class V chitinases from ''Nicotiana tabacum'' and ''Arabidopsis thaliana''. ''J Appl Glycosci'', 59, 1, 47-50 (2012)
# Umemoto N, Ohnuma T, Mizuhara M, Sato H, Skriver K, Fukamizo T. Introduction of a tryptophan side chain into subsite +1 enhances transglycosylation activity of a GH-18 chitinase from ''Arabidopsis thaliana'', AtChiC. ''Glycobiology'', 23, 81-90 (2013)
# Ohnuma T, Numata T, Osawa T, Inanaga H, Okazaki Y, Shinya S, Kondo K, Fukuda T, Fukamizo T. Crystal structure and chitin oligosaccharide-binding mode of a 'loopful' family GH19 chitinase from rye, ''Secale cereale'', seeds. ''FEBS J'', 19, 3639-3651 (2012)
# Umemoto N, Ohnuma T, Urpilainen H, Yamamoto T, Numata T, Fukamizo T. Role of tryptophan residues in a class V chitinase from ''Nicotiana tabacum''. ''Biosci Biotechnol Biochem'', 76,778-784 (2012)
# Ohnuma T, Fukuda T, Dozen S, Honda Y, Kitaoka M, Fukamizo T. A glycosynthase derived from an inverting GH19 chitinase from the moss ''Bryum coronatum''. ''Biochem J'', 444, 437-443 (2012)
# Shinya S, Ohnuma T, Kawamura S, Torikata T, Nishimura S, Katoh E, Fukamizo T. Interaction of a goose-type lysozyme with chitin oligosaccharides as determined by NMR spectroscopy. ''J Biochem'', 150, 569-577 (2011)
# Ohnuma T, Sørlie M, Fukuda T, Kawamoto N, Taira T, Fukamizo T. Chitin oligosaccharide binding to a family GH19 chitinase from the moss ''Bryum coronatum''. ''FEBS J'', 278, 3991-4001 (2011)
# Ohnuma T, Numata T, Osawa T, Mizuhara M, Lampela O, Juffer AH, Skriver K, Fukamizo T. A class V chitinase from ''Arabidopsis thaliana'': gene responses, enzymatic properties, and crystallographic analysis. ''Planta'', 234, 123-137 (2011)
# Ohnuma T, Numata T, Osawa T, Mizuhara M, Vårum KM, Fukamizo T. Crystal structure and mode of action of a class V chitinase from ''Nicotiana tabacum''. ''Plant Mol Biol'', 75, 291-304 (2011)
[[Category:Contributors|Ohnuma, Takayuki]]

User:Takayuki Ohnuma

2014-05-22T08:06:31Z

Takayuki Ohnuma:

[[Image:Taka.jpg|thumb|widthpx| ]]Takayuki Ohnuma is an assistant professor at Department of Advanced Bioscience, Faculty of Agriculture, Kinki University located in Nara, Japan.
He received PhD degree in 2002 from Graduate School of Agriculture in Kyushu University. His research program currently focuses on the structures and functions of plant chitinases (GH18 and GH19), including their CBMs (CBM18 and CBM50), which are involved in plant self-defense against fungal pathogens. In 2013, He and his colabolater published [9] the structure of a complex of rye family 19 chitinase with two molecules of (GlcNAc)4. This is the first report on the complete subsite mapping of GH19 chitinase.

References

1. Ohnuma T, Umemoto N, Nagata T, Shinya S, Numata T, Taira T, Fukamizo T. Crystal structure of a "loopless" GH19 chitinase in complex with chitin tetrasaccharide spanning the catalytic center. Biochim Biophys Acta, 1844, 793-802 (2014)

2. Ohnuma T, Umemoto N, Kondo K, Numata T, Fukamizo T. Complete subsite mapping of a "loopful" GH19 chitinase from rye seeds based on its crystal structure. FEBS Lett, 587, 2691-7 (2013)

3. Ohnuma T, Taira T, Fukamizo T. Antifungal activity of recombinant class V chitinases from Nicotiana tabacum and Arabidopsis thaliana. J Appl Glycosci, 59, 1, 47-50 (2012)

4. Umemoto N, Ohnuma T, Mizuhara M, Sato H, Skriver K, Fukamizo T. Introduction of a tryptophan side chain into subsite +1 enhances transglycosylation activity of a GH-18 chitinase from Arabidopsis thaliana, AtChiC. Glycobiology, 23, 81-90 (2013)

5. Ohnuma T, Numata T, Osawa T, Inanaga H, Okazaki Y, Shinya S, Kondo K, Fukuda T, Fukamizo T. Crystal structure and chitin oligosaccharide-binding mode of a 'loopful' family GH19 chitinase from rye, Secale cereale, seeds. FEBS J, 19, 3639-3651 (2012)

6. Umemoto N, Ohnuma T, Urpilainen H, Yamamoto T, Numata T, Fukamizo T. Role of tryptophan residues in a class V chitinase from Nicotiana tabacum. Biosci Biotechnol Biochem, 76,778-784 (2012)
7. Ohnuma T, Fukuda T, Dozen S, Honda Y, Kitaoka M, Fukamizo T. A glycosynthase derived from an inverting GH19 chitinase from the moss Bryum coronatum. Biochem J, 444, 437-443 (2012)

8. Shinya S, Ohnuma T, Kawamura S, Torikata T, Nishimura S, Katoh E, Fukamizo T. Interaction of a goose-type lysozyme with chitin oligosaccharides as determined by NMR spectroscopy. J Biochem, 150, 569-577 (2011)

9. Ohnuma T, Sørlie M, Fukuda T, Kawamoto N, Taira T, Fukamizo T. Chitin oligosaccharide binding to a family GH19 chitinase from the moss Bryum coronatum. FEBS J, 278, 3991-4001 (2011)

10. Ohnuma T, Numata T, Osawa T, Mizuhara M, Lampela O, Juffer AH, Skriver K, Fukamizo T. A class V chitinase from Arabidopsis thaliana: gene responses, enzymatic properties, and crystallographic analysis. Planta, 234, 123-137 (2011)

11. Ohnuma T, Numata T, Osawa T, Mizuhara M, Vårum KM, Fukamizo T. Crystal structure and mode of action of a class V chitinase from Nicotiana tabacum. Plant Mol Biol, 75, 291-304 (2011)
[[Category:Contributors|Ohnuma, Takayuki]]

User:Takayuki Ohnuma

2014-05-22T06:00:04Z

Takayuki Ohnuma:

Takayuki Ohnuma is an assistant professor at Department of Advanced Bioscience, Faculty of Agriculture, Kinki University located in Nara, Japan.
[[File:Taka.jpg]]He received PhD degree in 2002 from Graduate School of Agriculture in Kyushu University. His research program currently focuses on the structures and functions of plant chitinases (GH18 and GH19), including their CBMs (CBM18 and CBM50), which are involved in plant self-defense against fungal pathogens. In 2013, He and his colabolater published [9] the structure of a complex of rye family 19 chitinase with two molecules of (GlcNAc)4. This is the first report on the complete subsite mapping of GH19 chitinase.

References

1. Ohnuma T, Umemoto N, Nagata T, Shinya S, Numata T, Taira T, Fukamizo T. Crystal structure of a "loopless" GH19 chitinase in complex with chitin tetrasaccharide spanning the catalytic center. Biochim Biophys Acta, 1844, 793-802 (2014)

2. Ohnuma T, Umemoto N, Kondo K, Numata T, Fukamizo T. Complete subsite mapping of a "loopful" GH19 chitinase from rye seeds based on its crystal structure. FEBS Lett, 587, 2691-7 (2013)

3. Ohnuma T, Taira T, Fukamizo T. Antifungal activity of recombinant class V chitinases from Nicotiana tabacum and Arabidopsis thaliana. J Appl Glycosci, 59, 1, 47-50 (2012)

4. Umemoto N*, Ohnuma T*, Mizuhara M, Sato H, Skriver K, Fukamizo T. Introduction of a tryptophan side chain into subsite +1 enhances transglycosylation activity of a GH-18 chitinase from Arabidopsis thaliana, AtChiC. Glycobiology, 23, 81-90 (2013) (*equally contributed)

5. Ohnuma T, Numata T, Osawa T, Inanaga H, Okazaki Y, Shinya S, Kondo K, Fukuda T, Fukamizo T. Crystal structure and chitin oligosaccharide-binding mode of a 'loopful' family GH19 chitinase from rye, Secale cereale, seeds. FEBS J, 19, 3639-3651 (2012)

6. Umemoto N*, Ohnuma T*, Urpilainen H, Yamamoto T, Numata T, Fukamizo T. Role of tryptophan residues in a class V chitinase from Nicotiana tabacum. Biosci Biotechnol Biochem, 76,778-784 (2012) (equally contributed)

7. Ohnuma T, Fukuda T, Dozen S, Honda Y, Kitaoka M, Fukamizo T. A glycosynthase derived from an inverting GH19 chitinase from the moss Bryum coronatum. Biochem J, 444, 437-443 (2012)

8. Shinya S*, Ohnuma T*, Kawamura S, Torikata T, Nishimura S, Katoh E, Fukamizo T. Interaction of a goose-type lysozyme with chitin oligosaccharides as determined by NMR spectroscopy. J Biochem, 150, 569-577 (2011) (*equally contributed)

9. Ohnuma T, Sørlie M, Fukuda T, Kawamoto N, Taira T, Fukamizo T. Chitin oligosaccharide binding to a family GH19 chitinase from the moss Bryum coronatum. FEBS J, 278, 3991-4001 (2011)

10. Ohnuma T, Numata T, Osawa T, Mizuhara M, Lampela O, Juffer AH, Skriver K, Fukamizo T. A class V chitinase from Arabidopsis thaliana: gene responses, enzymatic properties, and crystallographic analysis. Planta, 234, 123-137 (2011)

11. Ohnuma T, Numata T, Osawa T, Mizuhara M, Vårum KM, Fukamizo T. Crystal structure and mode of action of a class V chitinase from Nicotiana tabacum. Plant Mol Biol, 75, 291-304 (2011) Normal 0 false 0 2 false false false EN-US JA X-NONE
[[Category:Contributors|Ohnuma, Takayuki]]

File:Taka.jpg

2014-05-22T05:58:05Z

Takayuki Ohnuma:

File:Takayuki.jpg

2014-05-22T05:42:30Z

Takayuki Ohnuma:

User:Takayuki Ohnuma

2014-05-22T05:15:27Z

Takayuki Ohnuma:

[[Image:filename|thumb|widthpx| ]]Takayuki Ohnuma is an assistant professor at Department of Advanced Bioscience, Faculty of Agriculture, Kinki University located in Nara, Japan. He received PhD degree in 2002 from Graduate School of Agriculture in Kyushu University. His research program currently focuses on the structures and functions of plant chitinases (GH18 and GH19), including their CBMs (CBM18 and CBM50), which are involved in plant self-defense against fungal pathogens. In 2013, He and his colabolater published [9] the structure of a complex of rye family 19 chitinase with two molecules of (GlcNAc)4. This is the first report on the complete subsite mapping of GH19 chitinase.

References

1. Ohnuma T, Umemoto N, Nagata T, Shinya S, Numata T, Taira T, Fukamizo T. Crystal structure of a "loopless" GH19 chitinase in complex with chitin tetrasaccharide spanning the catalytic center. Biochim Biophys Acta, 1844, 793-802 (2014)

2. Ohnuma T, Umemoto N, Kondo K, Numata T, Fukamizo T. Complete subsite mapping of a "loopful" GH19 chitinase from rye seeds based on its crystal structure. FEBS Lett, 587, 2691-7 (2013)

3. Ohnuma T, Taira T, Fukamizo T. Antifungal activity of recombinant class V chitinases from Nicotiana tabacum and Arabidopsis thaliana. J Appl Glycosci, 59, 1, 47-50 (2012)

4. Umemoto N*, Ohnuma T*, Mizuhara M, Sato H, Skriver K, Fukamizo T. Introduction of a tryptophan side chain into subsite +1 enhances transglycosylation activity of a GH-18 chitinase from Arabidopsis thaliana, AtChiC. Glycobiology, 23, 81-90 (2013) (*equally contributed)

5. Ohnuma T, Numata T, Osawa T, Inanaga H, Okazaki Y, Shinya S, Kondo K, Fukuda T, Fukamizo T. Crystal structure and chitin oligosaccharide-binding mode of a 'loopful' family GH19 chitinase from rye, Secale cereale, seeds. FEBS J, 19, 3639-3651 (2012)

6. Umemoto N*, Ohnuma T*, Urpilainen H, Yamamoto T, Numata T, Fukamizo T. Role of tryptophan residues in a class V chitinase from Nicotiana tabacum. Biosci Biotechnol Biochem, 76,778-784 (2012) (equally contributed)

7. Ohnuma T, Fukuda T, Dozen S, Honda Y, Kitaoka M, Fukamizo T. A glycosynthase derived from an inverting GH19 chitinase from the moss Bryum coronatum. Biochem J, 444, 437-443 (2012)

8. Shinya S*, Ohnuma T*, Kawamura S, Torikata T, Nishimura S, Katoh E, Fukamizo T. Interaction of a goose-type lysozyme with chitin oligosaccharides as determined by NMR spectroscopy. J Biochem, 150, 569-577 (2011) (*equally contributed)

9. Ohnuma T, Sørlie M, Fukuda T, Kawamoto N, Taira T, Fukamizo T. Chitin oligosaccharide binding to a family GH19 chitinase from the moss Bryum coronatum. FEBS J, 278, 3991-4001 (2011)

10. Ohnuma T, Numata T, Osawa T, Mizuhara M, Lampela O, Juffer AH, Skriver K, Fukamizo T. A class V chitinase from Arabidopsis thaliana: gene responses, enzymatic properties, and crystallographic analysis. Planta, 234, 123-137 (2011)

11. Ohnuma T, Numata T, Osawa T, Mizuhara M, Vårum KM, Fukamizo T. Crystal structure and mode of action of a class V chitinase from Nicotiana tabacum. Plant Mol Biol, 75, 291-304 (2011) Normal 0 false 0 2 false false false EN-US JA X-NONE
[[Category:Contributors|Ohnuma, Takayuki]]

File:Ohnuma.jpeg

2014-05-22T05:05:53Z

Takayuki Ohnuma:

User:Takayuki Ohnuma

2014-05-22T04:33:14Z

Takayuki Ohnuma:

Takayuki Ohnuma is an assistant professor at Department of Advanced Bioscience, Faculty of Agriculture, Kinki University located in Nara, Japan. He received PhD degree in 2002 from Graduate School of Agriculture in Kyushu University. His research program currently focuses on the structures and functions of plant chitinases (GH18 and GH19), including their CBMs (CBM18 and CBM50), which are involved in plant self-defense against fungal pathogens[1-11]. In 2013, He and his colabolater published [2] the structure of a complex of rye family 19 chitinase with two molecules of (GlcNAc)4. This is the first report on the complete subsite mapping of GH19 chitinase.

[[Category:Contributors|Ohnuma, Takayuki]]

User:Takayuki Ohnuma

2014-05-22T04:32:36Z

Takayuki Ohnuma: