| EC |
3.4.22.67 |
| Accepted name: |
zingipain |
| Reaction: |
Preferential cleavage of peptides with a proline residue at the P2 position |
| Other name(s): |
ginger protease; GP-I; GP-II; ginger protease II (Zingiber officinale); zingibain |
| Comments: |
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. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Choi, K.H. and Laursen, R.A. Amino-acid sequence and glycan structures of cysteine proteases with proline specificity from ginger rhizome Zingiber officinale. Eur. J. Biochem. 267 (2000) 1516–1526. [DOI] [PMID: 10691991] |
| 2. |
Ohtsuki, K., Taguchi, K., Sato, K. and Kawabata, M. Purification of ginger proteases by DEAE-Sepharose and isoelectric focusing. Biochim. Biophys. Acta 1243 (1995) 181–184. [DOI] [PMID: 7873561] |
| 3. |
Choi, K.H., Laursen, R.A. and Allen, K.N. The 2.1 Å structure of a cysteine protease with proline specificity from ginger rhizome, Zingiber officinale. Biochemistry 38 (1999) 11624–11633. [DOI] [PMID: 10512617] |
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| [EC 3.4.22.67 created 2007] |
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