Preferential cleavage of peptides with a proline residue at the P2 position
ginger protease; GP-I; GP-II; ginger protease II (Zingiber officinale); zingibain
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+ . Belongs in peptidase family C1.
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]
Ohtsuki, K., Taguchi, K., Sato, K. and Kawabata, M. Purification of ginger proteases by DEAE-Sepharose and isoelectric focusing. Biochim. Biophys. Acta1243 (1995) 181–184. [DOI] [PMID: 7873561]
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. Biochemistry38 (1999) 11624–11633. [DOI] [PMID: 10512617]