DB code: D00426

RLCP classification 1.13.30000.10 : Hydrolysis
CATH domain 2.40.10.10 : Thrombin, subunit H Catalytic domain
2.40.10.10 : Thrombin, subunit H Catalytic domain
E.C. 3.4.21.20
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
2.40.10.10 : Thrombin, subunit H M00139 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

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq MEROPS Pfam
P08311 Cathepsin G
CG
EC 3.4.21.20
NP_001902.1 (Protein)
NM_001911.2 (DNA/RNA sequence)
S01.133 (Serine)
PF00089 (Trypsin)
[Graphical View]

KEGG enzyme name
cathepsin G
chymotrypsin-like proteinase
neutral proteinase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P08311 CATG_HUMAN Specificity similar to chymotrypsin C.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C00017 C00012 C00001 C00098 C00012 I00087 I00085 I00086
E.C.
Compound Protein Peptide H2O Oligopeptide Peptide Peptidyl-tetrahedral intermediate Acyl-enzyme Tetrahedral intermediate
Type peptide/protein peptide/protein H2O amine group,carboxyl group,peptide/protein peptide/protein
ChEBI 15377
PubChem 22247451
962
1au8A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-analogue:SIN-VAL-PRO-KPH (chain S)
1cghA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-analogue:SIN-VAL-PRO-PPH (chain S)
1kynA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kynB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1au8A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cghA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kynA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1kynB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;1au8,1cgh & Swiss-prot;P08311

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1au8A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
1cghA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
1kynA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
1kynB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 495 GLY 493;SER 495
1au8A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
1cghA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
1kynA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
1kynB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 357;ASP 402

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[14]
p.5485-5486

References
[1]
Resource
Comments
Medline ID
PubMed ID 3266707
Journal Adv Exp Med Biol
Year 1988
Volume 240
Pages 23-31
Authors Watorek W, Farley D, Salvesen G, Travis J
Title Neutrophil elastase and cathepsin G: structure, function, and biological control.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 2516450
Journal Am J Respir Cell Mol Biol
Year 1989
Volume 1
Pages 37-9
Authors Pelletier A, Dimicoli JL, Boudier C, Bieth JG
Title Nonchromogenic hydrolysis of elastase and cathepsin G p-nitroanilide substrates by Pseudomonas aeruginosa elastase.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 2280356
Journal J Pharm Sci
Year 1990
Volume 79
Pages 886-8
Authors Groutas WC, Stanga MA, Castrisos JC, Schatz EJ, Brubaker MJ
Title Ionic inhibitors of human leukocyte elastase: pyridinium and phenyl carboxylate derivatives of 3-alkyl-N-hydroxysuccinimide.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 1988040
Journal Biochemistry
Year 1991
Volume 30
Pages 485-93
Authors Oleksyszyn J, Powers JC
Title Irreversible inhibition of serine proteases by peptide derivatives of (alpha-aminoalkyl)phosphonate diphenyl esters.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 1310061
Journal Blood
Year 1992
Volume 79
Pages 699-707
Authors Britigan BE, Roeder TL, Shasby DM
Title Insight into the nature and site of oxygen-centered free radical generation by endothelial cell monolayers using a novel spin trapping technique.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 1509406
Journal Thromb Haemost
Year 1992
Volume 67
Pages 660-4
Authors Evangelista V, Piccardoni P, de Gaetano G, Cerletti C
Title Defibrotide inhibits platelet activation by cathepsin G released from stimulated polymorphonuclear leukocytes.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 8357534
Journal Biol Chem Hoppe Seyler
Year 1993
Volume 374
Pages 385-93
Authors Watorek W, van Halbeek H, Travis J
Title The isoforms of human neutrophil elastase and cathepsin G differ in their carbohydrate side chain structures.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 8365692
Journal Haemostasis
Year 1993
Volume 23
Pages 98-103
Authors Turkington PT
Title Cathepsin G inactivates human protein S in vitro.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 7986820
Journal Biochim Biophys Acta
Year 1994
Volume 1227
Pages 130-6
Authors Groutas WC, Huang H, Epp JB, Venkataraman R, McClenahan JJ, Tagusagawa F
Title Mechanism-based inhibition of human leukocyte elastase and cathepsin G by substituted dihydrouracils.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 7925979
Journal FEBS Lett
Year 1994
Volume 352
Pages 231-5
Authors Padrines M, Wolf M, Walz A, Baggiolini M
Title Interleukin-8 processing by neutrophil elastase, cathepsin G and proteinase-3.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 7796053
Journal Bioorg Med Chem
Year 1995
Volume 3
Pages 187-93
Authors Groutas WC, Chong LS, Venkataraman R, Epp JB, Kuang R, Houser-Archield N, Hoidal JR
Title The 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.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 7796046
Journal Bioorg Med Chem
Year 1995
Volume 3
Pages 125-8
Authors Groutas WC, Venkataraman R, Chong LS, Yoder JE, Epp JB, Stanga MA, Kim EH
Title Isoxazoline derivatives as potential inhibitors of the proteolytic enzymes human leukocyte elastase, cathepsin G and proteinase 3: a structure-activity relationship study.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 8894097
Journal Bioorg Med Chem
Year 1996
Volume 4
Pages 1393-400
Authors Groutas WC, Epp JB, Venkataraman R, Kuang R, Truong TM, McClenahan JJ, Prakash O
Title Design, synthesis, and in vitro inhibitory activity toward human leukocyte elastase, cathepsin G, and proteinase 3 of saccharin-derived sulfones and congeners.
Related PDB
Related UniProtKB
[14]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
Medline ID 97051807
PubMed ID 8896442
Journal EMBO J
Year 1996
Volume 15
Pages 5481-91
Authors Hof P, Mayr I, Huber R, Korzus E, Potempa J, Travis J, Powers JC, Bode W
Title The 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 PDB 1cgh 1au8
Related UniProtKB P08311
[15]
Resource
Comments
Medline ID
PubMed ID 9125494
Journal Biochemistry
Year 1997
Volume 36
Pages 4739-50
Authors Groutas WC, Kuang R, Venkataraman R, Epp JB, Ruan S, Prakash O
Title Structure-based design of a general class of mechanism-based inhibitors of the serine proteinases employing a novel amino acid-derived heterocyclic scaffold.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 9370038
Journal Bioorg Med Chem
Year 1997
Volume 5
Pages 1935-42
Authors Gutschow M, Neumann U
Title Inhibition of cathepsin G by 4H-3,1-benzoxazin-4-ones.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 9242546
Journal Blood
Year 1997
Volume 90
Pages 1141-9
Authors McNeely TB, Shugars DC, Rosendahl M, Tucker C, Eisenberg SP, Wahl SM
Title Inhibition of human immunodeficiency virus type 1 infectivity by secretory leukocyte protease inhibitor occurs prior to viral reverse transcription.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 9718313
Journal Biochemistry
Year 1998
Volume 37
Pages 11896-906
Authors Camire RM, Kalafatis M, Tracy PB
Title Proteolysis of factor V by cathepsin G and elastase indicates that cleavage at Arg1545 optimizes cofactor function by facilitating factor Xa binding.
Related PDB
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 9570564
Journal J Immunol
Year 1998
Volume 160
Pages 1436-43
Authors Owen CA, Campbell EJ
Title Angiotensin II generation at the cell surface of activated neutrophils: novel cathepsin G-mediated catalytic activity that is resistant to inhibition.
Related PDB
Related UniProtKB
[20]
Resource
Comments
Medline ID
PubMed ID 10318785
Journal J Biol Chem
Year 1999
Volume 274
Pages 13810-7
Authors Rehault S, Brillard-Bourdet M, Juliano MA, Juliano L, Gauthier F, Moreau T
Title New, sensitive fluorogenic substrates for human cathepsin G based on the sequence of serpin-reactive site loops.
Related PDB
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 11101139
Journal Mol Cells
Year 2000
Volume 10
Pages 498-504
Authors Kim WM, Kang K
Title Enzymatic and molecular biochemical characterizations of human neutrophil elastases and a cathepsin G-like enzyme.
Related PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 10850807
Journal Protein Sci
Year 2000
Volume 9
Pages 976-84
Authors Cierpicki T, Bania J, Otlewski J
Title NMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1): structural similarity with Ascaris protease inhibitors.
Related PDB
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 11536009
Journal Cell Death Differ
Year 2001
Volume 8
Pages 588-94
Authors Gobeil S, Boucher CC, Nadeau D, Poirier GG
Title Characterization of the necrotic cleavage of poly(ADP-ribose) polymerase (PARP-1): implication of lysosomal proteases.
Related PDB
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 11942800
Journal J Am Chem Soc
Year 2002
Volume 124
Pages 3810-1
Authors Greco MN, Hawkins MJ, Powell ET, Almond HR Jr, Corcoran TW, de Garavilla L, Kauffman JA, Recacha R, Chattopadhyay D, Andrade-Gordon P, Maryanoff BE
Title Nonpeptide inhibitors of cathepsin G: optimization of a novel beta-ketophosphonic acid lead by structure-based drug design.
Related PDB 1kyn
Related UniProtKB

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.

Created Updated
2004-05-10 2011-02-17