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== Substrate specificities ==
 
== Substrate specificities ==
[[Glycoside hydrolases]] belonging to [[GH65]] act on substrates containing α-glucosidic linkages. [[GH65]] contains mainly [[phosphorylases]]; maltose (Glc-α-1,4-Glc) phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]), trehalose (Glc-α1,α1-Glc) phosphorylase (EC [{{EClink}}2.4.1.64 2.4.1.64]), kojibiose (Glc-α-1,2-Glc) phosphorylase (EC [{{EClink}}2.4.1.230 2.4.1.230]), and trehalose 6-phosphate (Glc-α1,α1-Glc6P) phosphorylase (EC [{{EClink}}2.4.1.- 2.4.1.-]). Noticeably α,α-trehalases (EC [{{EClink}}3.2.1.28 3.2.1.28]), a hydrolase, are also [[GH65]] members.
+
[[Glycoside hydrolases]] belonging to [[GH65]] act on substrates containing α-glucosidic linkages. [[GH65]] contains mainly [[phosphorylases]]; maltose (Glc-α-1,4-Glc) phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]), trehalose (Glc-α1,α1-Glc) phosphorylase (EC [{{EClink}}2.4.1.64 2.4.1.64]), kojibiose (Glc-α-1,2-Glc) phosphorylase (EC [{{EClink}}2.4.1.230 2.4.1.230]), and trehalose 6-phosphate (Glc-α1,α1-Glc6P) phosphorylase (EC [{{EClink}}2.4.1.- 2.4.1.-]). Noticeably α,α-trehalases (EC [{{EClink}}3.2.1.28 3.2.1.28]), a hydrolase, are also [[GH65]] members.
  
 
== Kinetics and Mechanism ==
 
== Kinetics and Mechanism ==
Phosphorolysis by [[GH65]] enzymes proceeds with [[inverting|inversion]] of anomeric configuration, as first shown by Fitting and Doudoroff <cite>Fitting1952</cite> using maltose phosphorylase from ''Neisseria meningitidis'', i.e. maltose + Pi ↔ β-glucose 1-phosphate + glucose. The reaction mechanism for [[inverting]] [[GH65]] phosphorylase has been proposed to be similar to a [[general acid/base]]-catalysed one-step displacement mechanism for inverting [[glycoside hydrolases]] <cite>Nakai2009</cite>. This mechanism was first proposed for [[inverting]] [[GH94]] phosphorylases (previously classified into glycoside transferase family 36) <cite>Hidaka2004</cite>, and involves direct nucleophilic attack by phosphate on the anomeric C1 carbon assisted by [[general acid]] catalysis involving protonation of the glycosidic oxygen. In this mechanism phosphate is the nucleophile, instead of a water molecule activated by a [[general base]] catalyst in [[inverting]] [[glycoside hydrolases]]. The inverting phosphorolysis catalyzed by GH65 enzyme is reversible, which confers the phosphorylase with a capacity to effectively synthesize various α-glucosides from β-glucose 1-phosphate as donor and acceptor molecules. Noticeably β-glucosyl fluoride can be used as donor in the synthetic reaction instead of the β-glucose 1-phosphate <cite>Tsumuraya1990</cite>.
+
Phosphorolysis by [[GH65]] enzymes proceeds with [[inverting|inversion]] of anomeric configuration, as first shown by Fitting and Doudoroff <cite>Fitting1952</cite> using maltose phosphorylase from ''Neisseria meningitidis'', i.e. maltose + Pi &harr; &beta;-glucose 1-phosphate + glucose. The reaction mechanism for [[inverting]] [[GH65]] phosphorylase has been proposed to be similar to a [[general acid/base]]-catalysed one-step displacement mechanism for inverting [[glycoside hydrolases]] <cite>Egloff2001 Nakai2009</cite>. This mechanism involves direct nucleophilic attack by phosphate on the anomeric C1 carbon assisted by [[general acid]] catalysis involving protonation of the glycosidic oxygen. In this mechanism phosphate is the nucleophile, instead of a water molecule activated by a [[general base]] catalyst in [[inverting]] [[glycoside hydrolases]]. Possibility of [[general base]] assistance by a histidine residue, which is located near the phosphate, is also suggested <cite>Egloff2001</cite>. The inverting phosphorolysis catalyzed by GH65 enzyme is reversible, which confers the phosphorylase with a capacity to effectively synthesize various &alpha;-glucosides from &beta;-glucose 1-phosphate as donor and acceptor molecules. Noticeably &beta;-glucosyl fluoride can be used as donor in the synthetic reaction instead of the &beta;-glucose 1-phosphate <cite>Tsumuraya1990</cite>.
  
 
== Catalytic Residues ==
 
== Catalytic Residues ==
The [[general acid]] catalyst was first predicted by superimposing the active site structure of maltose phosphorylase from ''Lactobacillus brevis'' <cite>Egloff2001</cite> with a catalytic (α/α)<sub>6</sub> barrel domain of GH15 glucoamylase (EC [{{EClink}}3.2.1.28 3.2.1.28]) from ''Aspergillus awamori'' <cite>Aleshin1992</cite>. Considering the similarities of the active site structure, Glu487 of ''L. brevis'' maltose phosphorylase was estimated as the [[general acid]]. Additionally it had been proved by site-direct mutagenesis on Glu487 of ''Paenibacillus'' sp. maltose phosphorylase <cite>Hidaka2005</cite>, which corresponds to the Glu487 of ''L. brevis'' maltose phosphorylase.
+
The [[general acid]] catalyst was first predicted by superimposing the active site structure of maltose phosphorylase from ''Lactobacillus brevis'' <cite>Egloff2001</cite> with a catalytic (&alpha;/&alpha;)<sub>6</sub> barrel domain of GH15 glucoamylase (EC [{{EClink}}3.2.1.28 3.2.1.28]) from ''Aspergillus awamori'' <cite>Aleshin1992</cite>. Considering the similarities of the active site structure, Glu487 of ''L. brevis'' maltose phosphorylase was estimated as the [[general acid]]. Additionally it had been proved by site-direct mutagenesis on Glu487 of ''Paenibacillus'' sp. maltose phosphorylase <cite>Hidaka2005</cite>, which corresponds to the Glu487 of ''L. brevis'' maltose phosphorylase. A histidine located near the phosphate (His671 in ''L. brevis'' maltose phosphorylase) could assist the catalysis as a [[general base]] <cite>Egloff2001</cite>, but no experimental evidences are shown.
  
 
== Three-dimensional structures ==
 
== Three-dimensional structures ==
The three-dimensional structure of ''L. brevis'' maltose phosphorylase (PDB ID [{{PDBlink}}1h54 1h54]) was determined <cite>Egloff2001</cite> and shows similarities with the (α/α)<sub>6</sub> barrel fold of [[GH15]] glucoamylase (EC [{{EClink}}3.2.1.28 3.2.1.28]) <cite>Aleshin1992</cite>, [[GH94]] cellobiose phosphorylase (EC [{{EClink}}2.4.1.20 2.4.1.20]) <cite>Hidaka2006</cite>, and [[GH94]] chitobiose phosphorylase (EC [{{EClink}}2.4.1.- 2.4.1.-]) <cite>Hidaka2004</cite>. [[GH15]] and [[GH65]] together constitute glycoside hydrolase clan L <cite>Cantarel2009</cite>.
+
[[Image:MalPstructure.png|'''Figure 1:''' Dimer structure of ''L. brevis'' maltose phosphorylase. <span style="color:#0000ff">An N-terminal complex &beta; sandwich domain is in blue</span>, <span style="color:#00cc00">a helical linkers in green</span>, <span style="color:#999900">an (&alpha;/&alpha;)<sub>6</sub> barrel catalytic domain is in yellow </span> and <span style="color:#ff0000"> a C-terminal &beta; sheet domain is in red </span>. <span style="color:#ff00ff">A phosphate molecule bound to chain B is shown as magenta spheres</span>.|frame|right]]
 +
The three-dimensional structure of ''L. brevis'' maltose phosphorylase (PDB ID [{{PDBlink}}1h54 1h54]) was firstly determined <cite>Egloff2001</cite>. ''L. brevis'' maltose phosphorylase is a dimeric enzyme ('''Figure 1'''). The monomer structure consists of an N-terminal complex &beta; sandwich domain, a helical linker, an (&alpha;/&alpha;)<sub>6</sub> barrel catalytic domain, and a C-terminal &beta; sheet domain. The structure of (&alpha;/&alpha;)<sub>6</sub> barrel domain is similar to [[GH15]] glucoamylase (EC [{{EClink}}3.2.1.28 3.2.1.28]) <cite>Aleshin1992</cite>. [[GH15]] and [[GH65]] together constitute glycoside hydrolase clan L <cite>Cantarel2009</cite>. [[GH94]] phosphorylases and a [[GH95]] fucosidase were also shown to be structurally similar to [[GH65]] <cite>Hidaka2004 Nagae2007</cite>.
  
 
== Family Firsts ==
 
== Family Firsts ==
;First stereochemistry determination: maltose phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]) from ''Neisseria meningitidis'' <cite>Fitting1952</cite>.
+
;First stereochemistry determination: Maltose phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]) from ''Neisseria meningitidis'' <cite>Fitting1952</cite>.
;First sequence identification: maltose phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]) from  ''Lactobacillus sanfranciscensis'' DSM 20451T <cite>Ehrmann1998</cite>
+
;First sequence identification: Maltose phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]) from  ''Lactobacillus sanfranciscensis'' DSM 20451T <cite>Ehrmann1998</cite>
: trehalose phosphorylase (EC [{{EClink}}2.4.1.64 2.4.1.64]) from ''Thermoanaerobacter brockii'' ATCC 35047 <cite> Maruta2002</cite>
+
: Trehalose phosphorylase (EC [{{EClink}}2.4.1.64 2.4.1.64]) from ''Thermoanaerobacter brockii'' ATCC 35047 <cite> Maruta2002</cite>
: kojibiose phosphorylase (EC [{{EClink}}2.4.1.230 2.4.1.230]) from ''Thermoanaerobacter brockii'' ATCC 35047 <cite>Yamatomo2004</cite>
+
: Kojibiose phosphorylase (EC [{{EClink}}2.4.1.230 2.4.1.230]) from ''Thermoanaerobacter brockii'' ATCC 35047 <cite>Yamatomo2004</cite>
: trehalose 6-phosphate phosphorylase (EC [{{EClink}}2.4.1.- 2.4.1.-]) from ''Lactococcus lactis'' ssp. ''lactis'' 19435 <cite> Andersson2001</cite>
+
: Trehalose 6-phosphate phosphorylase (EC [{{EClink}}2.4.1.- 2.4.1.-]) from ''Lactococcus lactis'' ssp. ''lactis'' 19435 <cite> Andersson2001</cite>
: α,α-trehalase (EC [{{EClink}}3.2.1.28 3.2.1.28]) from ''Saccharomyces cerevisiae'' S288C <cite>Destruelle1995</cite>.
+
: &alpha;,&alpha;-Trehalase (EC [{{EClink}}3.2.1.28 3.2.1.28]) from ''Saccharomyces cerevisiae'' S288C <cite>Destruelle1995</cite>.
;First [[general acid]] residue identification: maltose phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]) from ''Lactobacillus brevis'' by X-ray structure analysis <cite>Egloff2001</cite> and confirmed by mutagenesis for ''Paenibacillus'' sp. maltose phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]) <cite>Hidaka2005</cite>.
+
;First [[general acid]] residue identification: Maltose phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]) from ''Lactobacillus brevis'' by X-ray structure analysis <cite>Egloff2001</cite> and confirmed by mutagenesis for ''Paenibacillus'' sp. maltose phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]) <cite>Hidaka2005</cite>.
;First three-dimentional structure determination: maltose phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]) from ''Lactobacillus brevis'' <cite>Egloff2001</cite>.
+
;First three-dimentional structure determination: Maltose phosphorylase (EC [{{EClink}}2.4.1.8 2.4.1.8]) from ''Lactobacillus brevis'' <cite>Egloff2001</cite>.
  
 
== References ==
 
== References ==
Line 59: Line 60:
 
#Aleshin1992 pmid=1527049
 
#Aleshin1992 pmid=1527049
 
#Hidaka2005 Hidaka Y, Hatada Y, Akita M, Yoshida M, Nakamura N, Takada M, Nakakuki T, Ito S, and Horikoshi K. ''Maltose phosphorylase from a deep-sea Paenibacillus sp.: Enzymatic properties and nucleotide and amino-acid sequences.'' Enzyme and Microbial Technology, Volume 37, Issue 2, 1 July 2005, Pages 185-194. [http://dx.doi.org/10.1016/j.enzmictec.2005.02.010 doi:10.1016/j.enzmictec.2005.02.010]
 
#Hidaka2005 Hidaka Y, Hatada Y, Akita M, Yoshida M, Nakamura N, Takada M, Nakakuki T, Ito S, and Horikoshi K. ''Maltose phosphorylase from a deep-sea Paenibacillus sp.: Enzymatic properties and nucleotide and amino-acid sequences.'' Enzyme and Microbial Technology, Volume 37, Issue 2, 1 July 2005, Pages 185-194. [http://dx.doi.org/10.1016/j.enzmictec.2005.02.010 doi:10.1016/j.enzmictec.2005.02.010]
#Hidaka2006 pmid=16646954
 
 
#Cantarel2009 pmid=18838391
 
#Cantarel2009 pmid=18838391
 +
#Nagae2007 pmid=17459873
 +
 
#Ehrmann1998 pmid=9851037
 
#Ehrmann1998 pmid=9851037
 
#Maruta2002 pmid=12400703
 
#Maruta2002 pmid=12400703

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Glycoside Hydrolase Family GH65
Clan GH-L
Mechanism inverting
Active site residues known
CAZy DB link
http://www.cazy.org/GH65.html


Substrate specificities

Glycoside hydrolases belonging to GH65 act on substrates containing α-glucosidic linkages. GH65 contains mainly phosphorylases; maltose (Glc-α-1,4-Glc) phosphorylase (EC 2.4.1.8), trehalose (Glc-α1,α1-Glc) phosphorylase (EC 2.4.1.64), kojibiose (Glc-α-1,2-Glc) phosphorylase (EC 2.4.1.230), and trehalose 6-phosphate (Glc-α1,α1-Glc6P) phosphorylase (EC 2.4.1.-). Noticeably α,α-trehalases (EC 3.2.1.28), a hydrolase, are also GH65 members.

Kinetics and Mechanism

Phosphorolysis by GH65 enzymes proceeds with inversion of anomeric configuration, as first shown by Fitting and Doudoroff [1] using maltose phosphorylase from Neisseria meningitidis, i.e. maltose + Pi ↔ β-glucose 1-phosphate + glucose. The reaction mechanism for inverting GH65 phosphorylase has been proposed to be similar to a general acid/base-catalysed one-step displacement mechanism for inverting glycoside hydrolases [2, 3]. This mechanism involves direct nucleophilic attack by phosphate on the anomeric C1 carbon assisted by general acid catalysis involving protonation of the glycosidic oxygen. In this mechanism phosphate is the nucleophile, instead of a water molecule activated by a general base catalyst in inverting glycoside hydrolases. Possibility of general base assistance by a histidine residue, which is located near the phosphate, is also suggested [2]. The inverting phosphorolysis catalyzed by GH65 enzyme is reversible, which confers the phosphorylase with a capacity to effectively synthesize various α-glucosides from β-glucose 1-phosphate as donor and acceptor molecules. Noticeably β-glucosyl fluoride can be used as donor in the synthetic reaction instead of the β-glucose 1-phosphate [4].

Catalytic Residues

The general acid catalyst was first predicted by superimposing the active site structure of maltose phosphorylase from Lactobacillus brevis [2] with a catalytic (α/α)6 barrel domain of GH15 glucoamylase (EC 3.2.1.28) from Aspergillus awamori [5]. Considering the similarities of the active site structure, Glu487 of L. brevis maltose phosphorylase was estimated as the general acid. Additionally it had been proved by site-direct mutagenesis on Glu487 of Paenibacillus sp. maltose phosphorylase [6], which corresponds to the Glu487 of L. brevis maltose phosphorylase. A histidine located near the phosphate (His671 in L. brevis maltose phosphorylase) could assist the catalysis as a general base [2], but no experimental evidences are shown.

Three-dimensional structures

Figure 1: Dimer structure of L. brevis maltose phosphorylase. An N-terminal complex β sandwich domain is in blue, a helical linkers in green, an (α/α)6 barrel catalytic domain is in yellow and a C-terminal β sheet domain is in red . A phosphate molecule bound to chain B is shown as magenta spheres.

The three-dimensional structure of L. brevis maltose phosphorylase (PDB ID 1h54) was firstly determined [2]. L. brevis maltose phosphorylase is a dimeric enzyme (Figure 1). The monomer structure consists of an N-terminal complex β sandwich domain, a helical linker, an (α/α)6 barrel catalytic domain, and a C-terminal β sheet domain. The structure of (α/α)6 barrel domain is similar to GH15 glucoamylase (EC 3.2.1.28) [5]. GH15 and GH65 together constitute glycoside hydrolase clan L [7]. GH94 phosphorylases and a GH95 fucosidase were also shown to be structurally similar to GH65 [8, 9].

Family Firsts

First stereochemistry determination
Maltose phosphorylase (EC 2.4.1.8) from Neisseria meningitidis [1].
First sequence identification
Maltose phosphorylase (EC 2.4.1.8) from Lactobacillus sanfranciscensis DSM 20451T [10]
Trehalose phosphorylase (EC 2.4.1.64) from Thermoanaerobacter brockii ATCC 35047 [11]
Kojibiose phosphorylase (EC 2.4.1.230) from Thermoanaerobacter brockii ATCC 35047 [12]
Trehalose 6-phosphate phosphorylase (EC 2.4.1.-) from Lactococcus lactis ssp. lactis 19435 [13]
α,α-Trehalase (EC 3.2.1.28) from Saccharomyces cerevisiae S288C [14].
First general acid residue identification
Maltose phosphorylase (EC 2.4.1.8) from Lactobacillus brevis by X-ray structure analysis [2] and confirmed by mutagenesis for Paenibacillus sp. maltose phosphorylase (EC 2.4.1.8) [6].
First three-dimentional structure determination
Maltose phosphorylase (EC 2.4.1.8) from Lactobacillus brevis [2].

References

  1. FITTING C and DOUDOROFF M. (1952) Phosphorolysis of maltose by enzyme preparations from Neisseria meningitidis. J Biol Chem. 199, 153-63. PubMed ID:12999827 | HubMed [Fitting1952]
  2. Egloff MP, Uppenberg J, Haalck L, and van Tilbeurgh H. (2001) Crystal structure of maltose phosphorylase from Lactobacillus brevis: unexpected evolutionary relationship with glucoamylases. Structure. 9, 689-97. DOI:10.1016/s0969-2126(01)00626-8 | PubMed ID:11587643 | HubMed [Egloff2001]
  3. Nakai H, Baumann MJ, Petersen BO, Westphal Y, Schols H, Dilokpimol A, Hachem MA, Lahtinen SJ, Duus JØ, and Svensson B. (2009) The maltodextrin transport system and metabolism in Lactobacillus acidophilus NCFM and production of novel alpha-glucosides through reverse phosphorolysis by maltose phosphorylase. FEBS J. 276, 7353-65. DOI:10.1111/j.1742-4658.2009.07445.x | PubMed ID:19919544 | HubMed [Nakai2009]
  4. Tsumuraya Y, Brewer CF, and Hehre EJ. (1990) Substrate-induced activation of maltose phosphorylase: interaction with the anomeric hydroxyl group of alpha-maltose and alpha-D-glucose controls the enzyme's glucosyltransferase activity. Arch Biochem Biophys. 281, 58-65. DOI:10.1016/0003-9861(90)90412-r | PubMed ID:2143366 | HubMed [Tsumuraya1990]
  5. Aleshin A, Golubev A, Firsov LM, and Honzatko RB. (1992) Crystal structure of glucoamylase from Aspergillus awamori var. X100 to 2.2-A resolution. J Biol Chem. 267, 19291-8. DOI:10.2210/pdb1gly/pdb | PubMed ID:1527049 | HubMed [Aleshin1992]
  6. Hidaka Y, Hatada Y, Akita M, Yoshida M, Nakamura N, Takada M, Nakakuki T, Ito S, and Horikoshi K. Maltose phosphorylase from a deep-sea Paenibacillus sp.: Enzymatic properties and nucleotide and amino-acid sequences. Enzyme and Microbial Technology, Volume 37, Issue 2, 1 July 2005, Pages 185-194. doi:10.1016/j.enzmictec.2005.02.010
    [Hidaka2005]
  7. Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, and Henrissat B. (2009) The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 37, D233-8. DOI:10.1093/nar/gkn663 | PubMed ID:18838391 | HubMed [Cantarel2009]
  8. Hidaka M, Honda Y, Kitaoka M, Nirasawa S, Hayashi K, Wakagi T, Shoun H, and Fushinobu S. (2004) Chitobiose phosphorylase from Vibrio proteolyticus, a member of glycosyl transferase family 36, has a clan GH-L-like (alpha/alpha)(6) barrel fold. Structure. 12, 937-47. DOI:10.1016/j.str.2004.03.027 | PubMed ID:15274915 | HubMed [Hidaka2004]
  9. Nagae M, Tsuchiya A, Katayama T, Yamamoto K, Wakatsuki S, and Kato R. (2007) Structural basis of the catalytic reaction mechanism of novel 1,2-alpha-L-fucosidase from Bifidobacterium bifidum. J Biol Chem. 282, 18497-509. DOI:10.1074/jbc.M702246200 | PubMed ID:17459873 | HubMed [Nagae2007]
  10. Ehrmann MA and Vogel RF. (1998) Maltose metabolism of Lactobacillus sanfranciscensis: cloning and heterologous expression of the key enzymes, maltose phosphorylase and phosphoglucomutase. FEMS Microbiol Lett. 169, 81-6. DOI:10.1111/j.1574-6968.1998.tb13302.x | PubMed ID:9851037 | HubMed [Ehrmann1998]
  11. Maruta K, Mukai K, Yamashita H, Kubota M, Chaen H, Fukuda S, and Kurimoto M. (2002) Gene encoding a trehalose phosphorylase from Thermoanaerobacter brockii ATCC 35047. Biosci Biotechnol Biochem. 66, 1976-80. DOI:10.1271/bbb.66.1976 | PubMed ID:12400703 | HubMed [Maruta2002]
  12. Yamamoto T, Maruta K, Mukai K, Yamashita H, Nishimoto T, Kubota M, Fukuda S, Kurimoto M, and Tsujisaka Y. (2004) Cloning and sequencing of kojibiose phosphorylase gene from Thermoanaerobacter brockii ATCC35047. J Biosci Bioeng. 98, 99-106. DOI:10.1016/S1389-1723(04)70249-2 | PubMed ID:16233673 | HubMed [Yamatomo2004]
  13. Andersson U, Levander F, and Rådström P. (2001) Trehalose-6-phosphate phosphorylase is part of a novel metabolic pathway for trehalose utilization in Lactococcus lactis. J Biol Chem. 276, 42707-13. DOI:10.1074/jbc.M108279200 | PubMed ID:11553642 | HubMed [Andersson2001]
  14. Destruelle M, Holzer H, and Klionsky DJ. (1995) Isolation and characterization of a novel yeast gene, ATH1, that is required for vacuolar acid trehalase activity. Yeast. 11, 1015-25. DOI:10.1002/yea.320111103 | PubMed ID:7502577 | HubMed [Destruelle1995]
All Medline abstracts: PubMed | HubMed