Jump to content

Tannase

From Wikipedia, the free encyclopedia

This is an old revision of this page, as edited by BU RoBOT (talk | contribs) at 13:14, 10 August 2016 (References: Sort into more specific stub template based on presence in Category:EC 3.1 or subcategories (Task 25)). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

tannase
Identifiers
EC no.3.1.1.20
CAS no.9025-71-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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

  1. ^ Dyckerhoff H, 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.
  2. ^ Haslam E, Stangroom JE (April 1966). "The esterase and depsidase activities of tannase". Biochem. J. 99 (1): 28–31. PMC 1264952. PMID 5965343.
  3. ^ 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.