KEGG   ENZYME: 3.4.22.67Help
Entry
EC 3.4.22.67                Enzyme                                 

Name
zingipain;
ginger protease;
GP-I;
GP-II;
ginger protease II (Zingiber officinale);
zingibain
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Cysteine endopeptidases
BRITE hierarchy
Reaction(IUBMB)
Preferential cleavage of peptides with a proline residue at the P2 position
Comment
This enzyme is found in ginger (Zingiber officinale) rhizome and is a member of the papain family. GP-II contains two glycosylation sites. The enzyme is inhibited by some divalent metal ions, such as Hg2+, Cu2+, Cd2+ and Zn2+ [2]. Belongs in peptidase family C1.
History
EC 3.4.22.67 created 2007
Reference
1  [PMID:10691991]
  Authors
Choi KH, Laursen RA.
  Title
Amino-acid sequence and glycan structures of cysteine proteases with proline specificity from ginger rhizome Zingiber officinale.
  Journal
Eur. J. Biochem. 267 (2000) 1516-26.
  Sequence
Reference
2  [PMID:7873561]
  Authors
Ohtsuki K, Taguchi K, Sato K, Kawabata M.
  Title
Purification of ginger proteases by DEAE-Sepharose and isoelectric focusing.
  Journal
Biochim. Biophys. Acta. 1243 (1995) 181-4.
Reference
3  [PMID:10512617]
  Authors
Choi KH, Laursen RA, Allen KN.
  Title
The 2.1 A structure of a cysteine protease with proline specificity from ginger rhizome, Zingiber officinale.
  Journal
Biochemistry. 38 (1999) 11624-33.
  Sequence
[up:P82474]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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