New to the CAZy classification? Read this first.
Want to learn more about CAZypedia? Read the CAZypedia 10th anniversary article in Glycobiology.

Difference between revisions of "Carbohydrate Binding Module Family 16"

From CAZypedia
Jump to: navigation, search
Line 31: Line 31:
 
In the Man5A of ''Caldanaerobius polysaccharolyticus'', the deletion of both its CBM16s severely impairs the ability of the catalytic module ([[GH5]]) to bind cellulose <cite>Cann1999</cite>.
 
In the Man5A of ''Caldanaerobius polysaccharolyticus'', the deletion of both its CBM16s severely impairs the ability of the catalytic module ([[GH5]]) to bind cellulose <cite>Cann1999</cite>.
  
In the case of CgkA from Zobellia galactanivorans, the presence of the CBM16 is not required for the enzymatic activity on kappa-carrageenan, but has been shown to take part in  the processive mechanism of the catalytic module (GH16) <cite>Matard-Mann2017</cite>.
+
In the case of CgkA from ''Zobellia galactanivorans'', the presence of the CBM16 is not required for the enzymatic activity on kappa-carrageenan, but has been shown to take part in  the processive mechanism of the catalytic module ([[GH16]]) <cite>Matard-Mann2017</cite>.
  
Even if frequently found within the gene coding for alginate lyase from family PL18, it is absent in the mature form of the enzyme, and no role in alginate degradation has been found up to now <cite>Sim2017</cite>. A chaperon function of this N-terminal module has been proposed after observation that its deletion hindered the correct folding and activity of the catalytic module <cite>Dong2014</cite>.
+
Even if frequently found within the gene coding for alginate lyase from family [[PL18]], it is absent in the mature form of the enzyme, and no role in alginate degradation has been found up to now <cite>Sim2017</cite>. A chaperone function of this N-terminal module has been proposed after observation that its deletion hindered the correct folding and activity of the catalytic module <cite>Dong2014</cite>.
  
 
''Content in this section should include, in paragraph form, a description of:''
 
''Content in this section should include, in paragraph form, a description of:''

Revision as of 08:45, 8 February 2019

Under construction icon-blue-48px.png
This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.

CAZy DB link
http://www.cazy.org/CBM16.html

Ligand specificities

Family 16 CBMs (CAZy - CBM16) are found essentially in bacteria (with the exception of some CBM16 members in archaea). They are also found associated with catalytic modules belonging mainly to 4 families of CAZymes: GH5 mannanases [1, 2], GH16 kappa carrageenases [3, 4, 5], GH18 chitinases [6] and PL18 alginate lyases [7, 8]. Binding to glucomannan and kappa-carrageenan has been demonstrated [1, 2, 5]. CBM16 binding to glucomannan (mixed β-1,4-linked polymer contains both glucose and mannose) has been studied by mean of ITC (isothermal titration calorimetry) analysis and X-ray crystallography of complexes with pentomannan and pentoglucan [1, 2]. Conversely, binding to kappa-carrageenan has been shown by a double-blind approach using polysaccharide microarrays [5].


Structural Features

CBM16 is a type B CBM family, with a characteristic concave cleft, allowing the binding of substrate longer than triose. The ligand binding cleft shows some promiscuity as it can accommodate both pentoses (containing glucose and mannose), but only in the context of planar polymer like β-1,4-glucans, and not helical β-1,3-glucans [1]. The crystallographic structure determination of both CBMs from Caldanaerobius polysaccharolyticus (formerly Thermoanaerobacterium polysaccharolyticum) ManA revealed the importance of two aromatic residues in the binding cleft, as long as two stretches of polar residues on both sides of the cleft [1]. Affinity studies of targeted mutants for the predicted key resides confirmed the importance of two tryptophans (Trp-20 and Trp-125), and two glutamines (Gln-81 and Gln-93) [2].

Based on sequence similarity and conservation of secondary structure elements it has been proposed that, along with the CBM4, CBM17, CBM22 and CBM27 families, they form a superfamily [9].

Functionalities

In the Man5A of Caldanaerobius polysaccharolyticus, the deletion of both its CBM16s severely impairs the ability of the catalytic module (GH5) to bind cellulose [10].

In the case of CgkA from Zobellia galactanivorans, the presence of the CBM16 is not required for the enzymatic activity on kappa-carrageenan, but has been shown to take part in the processive mechanism of the catalytic module (GH16) [4].

Even if frequently found within the gene coding for alginate lyase from family PL18, it is absent in the mature form of the enzyme, and no role in alginate degradation has been found up to now [8]. A chaperone function of this N-terminal module has been proposed after observation that its deletion hindered the correct folding and activity of the catalytic module [7].

Content in this section should include, in paragraph form, a description of:

  • Functional role of CBM: Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.
  • Most Common Associated Modules: 1. Glycoside Hydrolase Activity; 2. Additional Associated Modules (other CBM, FNIII, cohesin, dockerins, expansins, etc.)
  • Novel Applications: Include here if CBM has been used to modify another enzyme, or if a CBM was used to label plant/mammalian tissues? Etc.

Family Firsts

First Identified

[10]: two CBM16 tandem associated, in C-terminal side of the Man5A GH5

First Structural Characterization

[1]

References

  1. pmid=
    [Bae2008]
  2. pmid=
    [Su2010]
  3. pmid=
    [Barbeyron1998]
  4. pmid=
    [Matard-Mann2017]
  5. pmid=
    [Salmean2017]
  6. pmid=
    [Barabote2009]
  7. pmid=
    [Dong2014]
  8. pmid=
    [Sim2017]
  9. pmid=
    [Sunna2001]
  10. pmid=
    [Cann1999]