Tannase
| tannase | |||||||||
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| Identifiers | |||||||||
| EC number | 3.1.1.20 | ||||||||
| CAS number | 9025-71-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
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In enzymology, a tannase (EC 3.1.1.20) is an enzyme that catalyzes the chemical reaction
- digallate + H2O
2 gallate
Thus, the two substrates of this enzyme are digallate and H2O, whereas its product is gallate.[1]
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is tannin acylhydrolase. Other names in common use include tannase S, and tannin acetylhydrolase.
In addition to catalyzing the hydrolysis of the central ester bond between the two aromatic rings of digallate (depsidase activity), tannase may also have an esterase activity (hydrolysis of terminal ester functional groups that are attached to only one of the two aromatic rings).[2]
Tannase is a key enzyme in the degradation of gallotannins, a type of hydrolysable tannins. It is present in a diverse group of microorganisms, including rumen bacteria.[3]
References
- ↑ Dyckerhoff H and Armbruster R (1933). "Zur Kenntnis der Tannase". Hoppe-Seyler's Z. Physiol. Chem. 219: 38–56. doi:10.1515/bchm2.1933.219.1-2.38.
- ↑ Haslam E, Stangroom JE (April 1966). "The esterase and depsidase activities of tannase". Biochem. J. 99 (1): 28–31. PMC 1264952. PMID 5965343.
- ↑ Bhat TK, Singh B, Sharma OP (1998). "Microbial degradation of tannins--a current perspective". Biodegradation 9 (5): 343–57. doi:10.1023/A:1008397506963. PMID 10192896.
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