EzCatDB: D00426
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DB codeD00426
RLCP classification1.13.30000.10 : Hydrolysis
CATH domainDomain 12.40.10.10 : Thrombin, subunit HCatalytic domain
Domain 22.40.10.10 : Thrombin, subunit HCatalytic domain
E.C.3.4.21.20

CATH domainRelated DB codes (homologues)
2.40.10.10 : Thrombin, subunit HM00139,D00214,M00167,M00133,D00428,D00429,D00430,D00431,D00432,D00433,D00434,D00435,M00227,M00209,D00194,D00197,D00211,D00212,D00216,M00212,D00224,D00497,M00217,M00216,D00528,D00848,D00850,D00851,D00852,D00855,M00152,M00155,M00157,M00181,M00315,M00316,M00317,M00348,M00349,T00074,T00410,T00411

Enzyme Name
UniProtKBKEGG

P08311
Protein nameCathepsin Gcathepsin G
chymotrypsin-like proteinase
neutral proteinase
SynonymsCG
EC 3.4.21.20
RefSeqNP_001902.1 (Protein)
NM_001911.2 (DNA/RNA sequence)
MEROPSS01.133 (Serine)
PfamPF00089 (Trypsin)
[Graphical view]


UniProtKB:Accession NumberP08311
Entry nameCATG_HUMAN
ActivitySpecificity similar to chymotrypsin C.
Subunit
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00017C00012C00001C00098C00012I00087I00085I00086
CompoundProteinPeptideH2OOligopeptidePeptidePeptidyl-tetrahedral intermediateAcyl-enzymeTetrahedral intermediate
Typepeptide/proteinpeptide/proteinH2Oamine group,carboxyl group,peptide/proteinpeptide/protein


ChEBI

15377





PubChem

962
22247451





                
1au8A01UnboundUnbound UnboundUnboundUnboundUnboundIntermediate-analogue:SIN-VAL-PRO-KPH(chain S)
1cghA01UnboundUnbound UnboundUnboundUnboundUnboundIntermediate-analogue:SIN-VAL-PRO-PPH(chain S)
1kynA01UnboundUnbound UnboundUnboundUnboundUnboundUnbound
1kynB01UnboundUnbound UnboundUnboundUnboundUnboundUnbound
1au8A02UnboundUnbound UnboundUnboundUnboundUnboundUnbound
1cghA02UnboundUnbound UnboundUnboundUnboundUnboundUnbound
1kynA02UnboundUnbound UnboundUnboundUnboundUnboundUnbound
1kynB02UnboundUnbound UnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
PDB;1au8,1cgh & Swiss-prot;P08311
pdbCatalytic residuesMain-chain involved in catalysis
          
1au8A01SER 195
GLY 193;SER 195
1cghA01SER 195
GLY 193;SER 195
1kynA01SER 195
GLY 193;SER 195
1kynB01SER 495
GLY 493;SER 495
1au8A02HIS  57;ASP 102
 
1cghA02HIS  57;ASP 102
 
1kynA02HIS  57;ASP 102
 
1kynB02HIS 357;ASP 402
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[14]p.5485-5486

references
[1]
PubMed ID3266707
JournalAdv Exp Med Biol
Year1988
Volume240
Pages23-31
AuthorsWatorek W, Farley D, Salvesen G, Travis J
TitleNeutrophil elastase and cathepsin G: structure, function, and biological control.
[2]
PubMed ID2516450
JournalAm J Respir Cell Mol Biol
Year1989
Volume1
Pages37-9
AuthorsPelletier A, Dimicoli JL, Boudier C, Bieth JG
TitleNonchromogenic hydrolysis of elastase and cathepsin G p-nitroanilide substrates by Pseudomonas aeruginosa elastase.
[3]
PubMed ID2280356
JournalJ Pharm Sci
Year1990
Volume79
Pages886-8
AuthorsGroutas WC, Stanga MA, Castrisos JC, Schatz EJ, Brubaker MJ
TitleIonic inhibitors of human leukocyte elastase: pyridinium and phenyl carboxylate derivatives of 3-alkyl-N-hydroxysuccinimide.
[4]
PubMed ID1988040
JournalBiochemistry
Year1991
Volume30
Pages485-93
AuthorsOleksyszyn J, Powers JC
TitleIrreversible inhibition of serine proteases by peptide derivatives of (alpha-aminoalkyl)phosphonate diphenyl esters.
[5]
PubMed ID1310061
JournalBlood
Year1992
Volume79
Pages699-707
AuthorsBritigan BE, Roeder TL, Shasby DM
TitleInsight into the nature and site of oxygen-centered free radical generation by endothelial cell monolayers using a novel spin trapping technique.
[6]
PubMed ID1509406
JournalThromb Haemost
Year1992
Volume67
Pages660-4
AuthorsEvangelista V, Piccardoni P, de Gaetano G, Cerletti C
TitleDefibrotide inhibits platelet activation by cathepsin G released from stimulated polymorphonuclear leukocytes.
[7]
PubMed ID8357534
JournalBiol Chem Hoppe Seyler
Year1993
Volume374
Pages385-93
AuthorsWatorek W, van Halbeek H, Travis J
TitleThe isoforms of human neutrophil elastase and cathepsin G differ in their carbohydrate side chain structures.
[8]
PubMed ID8365692
JournalHaemostasis
Year1993
Volume23
Pages98-103
AuthorsTurkington PT
TitleCathepsin G inactivates human protein S in vitro.
[9]
PubMed ID7986820
JournalBiochim Biophys Acta
Year1994
Volume1227
Pages130-6
AuthorsGroutas WC, Huang H, Epp JB, Venkataraman R, McClenahan JJ, Tagusagawa F
TitleMechanism-based inhibition of human leukocyte elastase and cathepsin G by substituted dihydrouracils.
[10]
PubMed ID7925979
JournalFEBS Lett
Year1994
Volume352
Pages231-5
AuthorsPadrines M, Wolf M, Walz A, Baggiolini M
TitleInterleukin-8 processing by neutrophil elastase, cathepsin G and proteinase-3.
[11]
PubMed ID7796053
JournalBioorg Med Chem
Year1995
Volume3
Pages187-93
AuthorsGroutas WC, Chong LS, Venkataraman R, Epp JB, Kuang R, Houser-Archield N, Hoidal JR
TitleThe Gabriel-Colman rearrangement in biological systems: design, synthesis and biological evaluation of phthalimide and saccharin derivatives as potential mechanism-based inhibitors of human leukocyte elastase, cathepsin G and proteinase 3.
[12]
PubMed ID7796046
JournalBioorg Med Chem
Year1995
Volume3
Pages125-8
AuthorsGroutas WC, Venkataraman R, Chong LS, Yoder JE, Epp JB, Stanga MA, Kim EH
TitleIsoxazoline derivatives as potential inhibitors of the proteolytic enzymes human leukocyte elastase, cathepsin G and proteinase 3: a structure-activity relationship study.
[13]
PubMed ID8894097
JournalBioorg Med Chem
Year1996
Volume4
Pages1393-400
AuthorsGroutas WC, Epp JB, Venkataraman R, Kuang R, Truong TM, McClenahan JJ, Prakash O
TitleDesign, synthesis, and in vitro inhibitory activity toward human leukocyte elastase, cathepsin G, and proteinase 3 of saccharin-derived sulfones and congeners.
[14]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
Medline ID97051807
PubMed ID8896442
JournalEMBO J
Year1996
Volume15
Pages5481-91
AuthorsHof P, Mayr I, Huber R, Korzus E, Potempa J, Travis J, Powers JC, Bode W
TitleThe 1.8 A crystal structure of human cathepsin G in complex with Suc-Val-Pro-PheP-(OPh)2: a Janus-faced proteinase with two opposite specificities.
Related PDB1cgh,1au8
Related UniProtKBP08311
[15]
PubMed ID9125494
JournalBiochemistry
Year1997
Volume36
Pages4739-50
AuthorsGroutas WC, Kuang R, Venkataraman R, Epp JB, Ruan S, Prakash O
TitleStructure-based design of a general class of mechanism-based inhibitors of the serine proteinases employing a novel amino acid-derived heterocyclic scaffold.
[16]
PubMed ID9370038
JournalBioorg Med Chem
Year1997
Volume5
Pages1935-42
AuthorsGutschow M, Neumann U
TitleInhibition of cathepsin G by 4H-3,1-benzoxazin-4-ones.
[17]
PubMed ID9242546
JournalBlood
Year1997
Volume90
Pages1141-9
AuthorsMcNeely TB, Shugars DC, Rosendahl M, Tucker C, Eisenberg SP, Wahl SM
TitleInhibition of human immunodeficiency virus type 1 infectivity by secretory leukocyte protease inhibitor occurs prior to viral reverse transcription.
[18]
PubMed ID9718313
JournalBiochemistry
Year1998
Volume37
Pages11896-906
AuthorsCamire RM, Kalafatis M, Tracy PB
TitleProteolysis of factor V by cathepsin G and elastase indicates that cleavage at Arg1545 optimizes cofactor function by facilitating factor Xa binding.
[19]
PubMed ID9570564
JournalJ Immunol
Year1998
Volume160
Pages1436-43
AuthorsOwen CA, Campbell EJ
TitleAngiotensin II generation at the cell surface of activated neutrophils: novel cathepsin G-mediated catalytic activity that is resistant to inhibition.
[20]
PubMed ID10318785
JournalJ Biol Chem
Year1999
Volume274
Pages13810-7
AuthorsRehault S, Brillard-Bourdet M, Juliano MA, Juliano L, Gauthier F, Moreau T
TitleNew, sensitive fluorogenic substrates for human cathepsin G based on the sequence of serpin-reactive site loops.
[21]
PubMed ID11101139
JournalMol Cells
Year2000
Volume10
Pages498-504
AuthorsKim WM, Kang K
TitleEnzymatic and molecular biochemical characterizations of human neutrophil elastases and a cathepsin G-like enzyme.
[22]
PubMed ID10850807
JournalProtein Sci
Year2000
Volume9
Pages976-84
AuthorsCierpicki T, Bania J, Otlewski J
TitleNMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1): structural similarity with Ascaris protease inhibitors.
[23]
PubMed ID11536009
JournalCell Death Differ
Year2001
Volume8
Pages588-94
AuthorsGobeil S, Boucher CC, Nadeau D, Poirier GG
TitleCharacterization of the necrotic cleavage of poly(ADP-ribose) polymerase (PARP-1): implication of lysosomal proteases.
[24]
PubMed ID11942800
JournalJ Am Chem Soc
Year2002
Volume124
Pages3810-1
AuthorsGreco MN, Hawkins MJ, Powell ET, Almond HR Jr, Corcoran TW, de Garavilla L, Kauffman JA, Recacha R, Chattopadhyay D, Andrade-Gordon P, Maryanoff BE
TitleNonpeptide inhibitors of cathepsin G: optimization of a novel beta-ketophosphonic acid lead by structure-based drug design.
Related PDB1kyn

comments
This enzyme belongs to the peptidase family-S1.
According to the literature [14], this enzyme has got a similar catalytic triad (Ser/His/Asp) and an oxyanion hole, to that of trypsin, suggesting a similar mechanism.

createdupdated
2004-05-102011-02-17


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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