Amino-acid sequence and glycan structures of cysteine proteases with proline specificity from ginger rhizome Zingiber officinale

Kyung Choi, Richard A. Laursen

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

The ginger proteases (GP-I and GP-II), isolated from the ginger rhizome Zingiber officinale, have an unusual substrate specificity preference for cleaving peptides with a proline residue at the P2 position. The complete amino-acid sequence of GP-II, a glycoprotein containing 221 amino acids, and about 98% that of GP-I have been determined. Both proteases, which are 82% similar, have cysteine residues at positions 27 and histidines at position 161, corresponding to the essential cysteine-histidine diads found in the papain family of cysteine proteases, and six corresponding cysteine residues that form the three invariant disulfide linkages seen in this family of proteins. The sequence homology with other members (papain, bromelain, actinidin, protease omega, etc.) of this family is ≃ 50%. GP-II has two predicted glycosylation sites at Asn99 and Asn156. Analysis by electrospray and collision-induced dissociation MS showed that both sites were occupied by the glycans (Man)3(Xyl)1(Fuc)1(GlcNAc)2 and (Man)3(Xyl)1(Fuc)1(GlcNAc)3, in a ratio of ≃ 7: 1. Both glycans are xylose containing biantennary complex types that share the common core structural unit, Man1→6(Man1→3) (Xy11→2)Man1→4GlcNAc1→4(Fuc1→3)GlcNAc for the major form, with an additional N-acetylglucosamine residue being linked, in the minor form, to one of the terminal mannose units of the core structure.

Original languageEnglish (US)
Pages (from-to)1516-1526
Number of pages11
JournalEuropean Journal of Biochemistry
Volume267
Issue number5
DOIs
StatePublished - 2000
Externally publishedYes

Fingerprint

Ginger
Rhizome
Cysteine Proteases
Proline
Polysaccharides
Cysteine
Amino Acid Sequence
Peptide Hydrolases
Papain
actinidain
Histidine
Amino Acids
Bromelains
Glycosylation
Acetylglucosamine
Xylose
Mannose
Sequence Homology
Substrate Specificity
Disulfides

Keywords

  • Amino-acid sequence
  • Cysteine protease
  • Ginger
  • Glycoprotein
  • Glycosylation site
  • Mass spectrometry
  • Proline peptidase
  • Proteinase

ASJC Scopus subject areas

  • Biochemistry

Cite this

Amino-acid sequence and glycan structures of cysteine proteases with proline specificity from ginger rhizome Zingiber officinale. / Choi, Kyung; Laursen, Richard A.

In: European Journal of Biochemistry, Vol. 267, No. 5, 2000, p. 1516-1526.

Research output: Contribution to journalArticle

@article{0bc79b26979448ae9f79d7a7335ec4e9,
title = "Amino-acid sequence and glycan structures of cysteine proteases with proline specificity from ginger rhizome Zingiber officinale",
abstract = "The ginger proteases (GP-I and GP-II), isolated from the ginger rhizome Zingiber officinale, have an unusual substrate specificity preference for cleaving peptides with a proline residue at the P2 position. The complete amino-acid sequence of GP-II, a glycoprotein containing 221 amino acids, and about 98{\%} that of GP-I have been determined. Both proteases, which are 82{\%} similar, have cysteine residues at positions 27 and histidines at position 161, corresponding to the essential cysteine-histidine diads found in the papain family of cysteine proteases, and six corresponding cysteine residues that form the three invariant disulfide linkages seen in this family of proteins. The sequence homology with other members (papain, bromelain, actinidin, protease omega, etc.) of this family is ≃ 50{\%}. GP-II has two predicted glycosylation sites at Asn99 and Asn156. Analysis by electrospray and collision-induced dissociation MS showed that both sites were occupied by the glycans (Man)3(Xyl)1(Fuc)1(GlcNAc)2 and (Man)3(Xyl)1(Fuc)1(GlcNAc)3, in a ratio of ≃ 7: 1. Both glycans are xylose containing biantennary complex types that share the common core structural unit, Man1→6(Man1→3) (Xy11→2)Man1→4GlcNAc1→4(Fuc1→3)GlcNAc for the major form, with an additional N-acetylglucosamine residue being linked, in the minor form, to one of the terminal mannose units of the core structure.",
keywords = "Amino-acid sequence, Cysteine protease, Ginger, Glycoprotein, Glycosylation site, Mass spectrometry, Proline peptidase, Proteinase",
author = "Kyung Choi and Laursen, {Richard A.}",
year = "2000",
doi = "10.1046/j.1432-1327.2000.01152.x",
language = "English (US)",
volume = "267",
pages = "1516--1526",
journal = "FEBS Journal",
issn = "1742-464X",
publisher = "Wiley-Blackwell",
number = "5",

}

TY - JOUR

T1 - Amino-acid sequence and glycan structures of cysteine proteases with proline specificity from ginger rhizome Zingiber officinale

AU - Choi, Kyung

AU - Laursen, Richard A.

PY - 2000

Y1 - 2000

N2 - The ginger proteases (GP-I and GP-II), isolated from the ginger rhizome Zingiber officinale, have an unusual substrate specificity preference for cleaving peptides with a proline residue at the P2 position. The complete amino-acid sequence of GP-II, a glycoprotein containing 221 amino acids, and about 98% that of GP-I have been determined. Both proteases, which are 82% similar, have cysteine residues at positions 27 and histidines at position 161, corresponding to the essential cysteine-histidine diads found in the papain family of cysteine proteases, and six corresponding cysteine residues that form the three invariant disulfide linkages seen in this family of proteins. The sequence homology with other members (papain, bromelain, actinidin, protease omega, etc.) of this family is ≃ 50%. GP-II has two predicted glycosylation sites at Asn99 and Asn156. Analysis by electrospray and collision-induced dissociation MS showed that both sites were occupied by the glycans (Man)3(Xyl)1(Fuc)1(GlcNAc)2 and (Man)3(Xyl)1(Fuc)1(GlcNAc)3, in a ratio of ≃ 7: 1. Both glycans are xylose containing biantennary complex types that share the common core structural unit, Man1→6(Man1→3) (Xy11→2)Man1→4GlcNAc1→4(Fuc1→3)GlcNAc for the major form, with an additional N-acetylglucosamine residue being linked, in the minor form, to one of the terminal mannose units of the core structure.

AB - The ginger proteases (GP-I and GP-II), isolated from the ginger rhizome Zingiber officinale, have an unusual substrate specificity preference for cleaving peptides with a proline residue at the P2 position. The complete amino-acid sequence of GP-II, a glycoprotein containing 221 amino acids, and about 98% that of GP-I have been determined. Both proteases, which are 82% similar, have cysteine residues at positions 27 and histidines at position 161, corresponding to the essential cysteine-histidine diads found in the papain family of cysteine proteases, and six corresponding cysteine residues that form the three invariant disulfide linkages seen in this family of proteins. The sequence homology with other members (papain, bromelain, actinidin, protease omega, etc.) of this family is ≃ 50%. GP-II has two predicted glycosylation sites at Asn99 and Asn156. Analysis by electrospray and collision-induced dissociation MS showed that both sites were occupied by the glycans (Man)3(Xyl)1(Fuc)1(GlcNAc)2 and (Man)3(Xyl)1(Fuc)1(GlcNAc)3, in a ratio of ≃ 7: 1. Both glycans are xylose containing biantennary complex types that share the common core structural unit, Man1→6(Man1→3) (Xy11→2)Man1→4GlcNAc1→4(Fuc1→3)GlcNAc for the major form, with an additional N-acetylglucosamine residue being linked, in the minor form, to one of the terminal mannose units of the core structure.

KW - Amino-acid sequence

KW - Cysteine protease

KW - Ginger

KW - Glycoprotein

KW - Glycosylation site

KW - Mass spectrometry

KW - Proline peptidase

KW - Proteinase

UR - http://www.scopus.com/inward/record.url?scp=0034015436&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034015436&partnerID=8YFLogxK

U2 - 10.1046/j.1432-1327.2000.01152.x

DO - 10.1046/j.1432-1327.2000.01152.x

M3 - Article

C2 - 10691991

AN - SCOPUS:0034015436

VL - 267

SP - 1516

EP - 1526

JO - FEBS Journal

JF - FEBS Journal

SN - 1742-464X

IS - 5

ER -