KEGG   ENZYME: 3.4.22.37
Entry
EC 3.4.22.37                Enzyme                                 
Name
gingipain R;
Arg-gingipain;
gingipain-1;
argingipain;
Arg-gingivain-55 proteinase;
Arg-gingivain-70 proteinase;
Arg-gingivain-75 proteinase;
arginine-specific cysteine protease;
arginine-specific gingipain;
arginine-specific gingivain;
RGP-1;
RGP
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Cysteine endopeptidases
Reaction(IUBMB)
Hydrolysis of proteins and small molecule substrates, with a preference for Arg in P1
Comment
A secreted endopeptidase from the bacterium Porphyromonas gingivalis. Strongly activated by glycine [1], and stabilized by Ca2+. Precursor molecule contains a hemagglutinin domain [2,3]. Misleadingly described in some literature as "trypsin-like", being a cysteine peptidase, type example of peptidase family C25.
History
EC 3.4.22.37 created 1996
Orthology
K08589  gingipain R
Genes
VPY: HZI73_06705
AMIC: Ami3637_15535
PGI: PG_0506(prtRII) PG_2024(hagE)
PGN: PGN_1466(rgpB) PGN_1970(rgpA)
PGT: PGTDC60_0300(rgpA) PGTDC60_1623(rgpB)
PNI: J5A59_06935
PMUF: J4864_03480
FALB: HYN59_01025
Reference
1  [PMID:1527017]
  Authors
Chen Z, Potempa J, Polanowski A, Wikstrom M, Travis J.
  Title
Purification and characterization of a 50-kDa cysteine proteinase (gingipain) from Porphyromonas gingivalis.
  Journal
J Biol Chem 267:18896-901 (1992)
  Sequence
[pgi:PG_2024]
Reference
2  [PMID:7857299]
  Authors
Kirszbaum L, Sotiropoulos C, Jackson C, Cleal S, Slakeski N, Reynolds EC
  Title
Complete nucleotide sequence of a gene prtR of Porphyromonas gingivalis W50 encoding a 132 kDa protein that contains an arginine-specific thiol endopeptidase domain and a haemagglutinin domain.
  Journal
Biochem Biophys Res Commun 207:424-31 (1995)
DOI:10.1006/bbrc.1995.1205
  Sequence
[pgi:PG_2024]
Reference
3  [PMID:7836351]
  Authors
Pavloff N, Potempa J, Pike RN, Prochazka V, Kiefer MC, Travis J, Barr PJ.
  Title
Molecular cloning and structural characterization of the Arg-gingipain proteinase of Porphyromonas gingivalis. Biosynthesis as a proteinase-adhesin polyprotein.
  Journal
J Biol Chem 270:1007-10 (1995)
DOI:10.1074/jbc.270.3.1007
  Sequence
[pgi:PG_2024]
Other DBs
ExplorEnz - The Enzyme Database: 3.4.22.37
IUBMB Enzyme Nomenclature: 3.4.22.37
ExPASy - ENZYME nomenclature database: 3.4.22.37
BRENDA, the Enzyme Database: 3.4.22.37
CAS: 159745-71-8

  All links  
Gene (12)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (11)   
Protein sequence (213)   
   UniProt (116)   
   SWISS-PROT (4)   
   RefSeq(pep) (78)   
   PDBSTR (15)   
DNA sequence (166)   
   RefSeq(nuc) (88)   
   GenBank (39)   
   EMBL (39)   
3D Structure (5)   
   PDB (5)   
Protein domain (13)   
   InterPro (13)   
All databases (409)   

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