Auxiliary Activity Family 10

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• Author: ^^^Vincent Eijsink^^^ and ^^^Gustav Vaaje-Kolstad^^^
• Responsible Curator: ^^^Vincent Eijsink^^^

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Auxiliary Activity Family 10
Clan	none, structurally related to AA9
Mechanism	lytic oxidase
Active site residues	mononuclear copper ion
CAZy DB link
http://www.cazy.org/AA10.html

Substrate specificities

So far AA10s have been shown to target chitin and cellulose, but binding has also been demonstrated for chitosan, bacterial surfaces....

Before the proteins belonging to AA10 were identified as enzymes, they were known as chitin binding proteins (CBPs). The reason for this is that most characterized proteins had been identified in chitinolytic systems such as that of Serratia marcescens (REF), several Streptomyces species (REFs), ......, and show no other obvious function than just binding the substrate. Thus there exists several papers that have analyzed the binding preferences of AA10s.

Shortly after CBP21 from S. marcescens was shown to specifically cleave chitin chains [1], CelS2 from Streptomyces coelicolor (also known as ScAA10D) was shown to act specifically on cellulose by a apparently identical monooxygenase activity [2]. In contrast to CBP21, which is a single AA10 module that binds strongly to beta-chitin, CelS2 has a CBM2 attached to the C-terminal side of the AA10 module that specifies binding of the enzyme cellulose.

Please see these references for an essential introduction to the CAZy classification system: [3, 4].

Kinetics and Mechanism

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Catalytic Residues

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Three-dimensional structures

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Family Firsts

First stereochemistry determination

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First catalytic nucleophile identification

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First general acid/base residue identification

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First 3-D structure

CBP21, the single AA10-type LPMO from the Gram negative bacterium Serratia marcescens. Entry in the protein data bank: [1]

References

1. Vaaje-Kolstad G, Westereng B, Horn SJ, Liu Z, Zhai H, Sørlie M, and Eijsink VG. (2010). An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides. Science. 2010;330(6001):219-22. DOI:10.1126/science.1192231 |
2. Forsberg Z, Vaaje-Kolstad G, Westereng B, Bunæs AC, Stenstrøm Y, MacKenzie A, Sørlie M, Horn SJ, and Eijsink VG. (2011). Cleavage of cellulose by a CBM33 protein. Protein Sci. 2011;20(9):1479-83. DOI:10.1002/pro.689 |

3. Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. Biochem. J. (BJ Classic Paper, online only). DOI: 10.1042/BJ20080382

4. 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. 2009;37(Database issue):D233-8. DOI:10.1093/nar/gkn663 |