EzCatDB: D00431
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DB codeD00431
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.3.4.21.59

CATH domainRelated DB codes (homologues)
2.40.10.10 : Thrombin, subunit HM00139,D00214,M00167,D00426,M00133,D00428,D00429,D00430,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

P20231
Protein nameTryptase beta-2tryptase
mast cell tryptase
mast cell protease II
skin tryptase
lung tryptase
pituitary tryptase
mast cell neutral proteinase
mast cell tryptase
mast cell neutral proteinase
mast cell serine proteinase II
mast cell proteinase II
mast cell serine proteinase tryptase
rat mast cell protease II
tryptase M
SynonymsTryptase-2
EC 3.4.21.59
Tryptase II
RefSeqNP_003285.2 (Protein)
NM_003294.3 (DNA/RNA sequence)
NP_077078.5 (Protein)
NM_024164.5 (DNA/RNA sequence)
MEROPSS01.015 (Serine)
PfamPF00089 (Trypsin)
[Graphical view]


UniProtKB:Accession NumberP20231
Entry nameTRYB2_HUMAN
ActivityPreferential cleavage: Arg-|-Xaa, Lys-|-Xaa, but with more restricted specificity than trypsin.
SubunitHomotetramer.
Subcellular locationSecreted. Note=Released from the secretory granules upon mast cell activation.
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00012C00017C00001C00012C00017I00087I00085I00086
CompoundPeptideProteinH2OPeptideProteinPeptidyl-tetrahedral intermediateAcyl-enzymeTetrahedral intermediate
Typepeptide/proteinpeptide/proteinH2Opeptide/proteinpeptide/protein


ChEBI

15377





PubChem

962
22247451





                
1a0lA01UnboundUnbound UnboundUnboundIntermediate-analogue:APAUnboundUnbound
1a0lB01UnboundUnbound UnboundUnboundIntermediate-analogue:APAUnboundUnbound
1a0lC01UnboundUnbound UnboundUnboundIntermediate-analogue:APAUnboundUnbound
1a0lD01UnboundUnbound UnboundUnboundIntermediate-analogue:APAUnboundUnbound
1a0lA02UnboundUnbound UnboundUnboundUnboundUnboundUnbound
1a0lB02UnboundUnbound UnboundUnboundUnboundUnboundUnbound
1a0lC02UnboundUnbound UnboundUnboundUnboundUnboundUnbound
1a0lD02UnboundUnbound UnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P20231
pdbCatalytic residuesMain-chain involved in catalysis
          
1a0lA01SER 195
GLY 193;SER 195
1a0lB01SER 195
GLY 193;SER 195
1a0lC01SER 195
GLY 193;SER 195
1a0lD01SER 195
GLY 193;SER 195
1a0lA02HIS  57;ASP 102
 
1a0lB02HIS  57;ASP 102
 
1a0lC02HIS  57;ASP 102
 
1a0lD02HIS  57;ASP 102
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[4]p.17079
[6]p.309

references
[1]
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.
[2]
PubMed ID9242660
JournalJ Biol Chem
Year1997
Volume272
Pages19931-7
AuthorsStubbs MT, Morenweiser R, Sturzebecher J, Bauer M, Bode W, Huber R, Piechottka GP, Matschiner G, Sommerhoff CP, Fritz H, Auerswald EA
TitleThe three-dimensional structure of recombinant leech-derived tryptase inhibitor in complex with trypsin. Implications for the structure of human mast cell tryptase and its inhibition.
[3]
PubMed ID9317153
JournalJ Immunol
Year1997
Volume159
Pages3540-8
AuthorsRen S, Lawson AE, Carr M, Baumgarten CM, Schwartz LB
TitleHuman tryptase fibrinogenolysis is optimal at acidic pH and generates anticoagulant fragments in the presence of the anti-tryptase monoclonal antibody B12.
[4]
PubMed ID9836602
JournalBiochemistry
Year1998
Volume37
Pages17068-81
AuthorsPresnell SR, Patil GS, Mura C, Jude KM, Conley JM, Bertrand JA, Kam CM, Powers JC, Williams LD
TitleOxyanion-mediated inhibition of serine proteases.
[5]
PubMed ID10197050
JournalCurr Pharm Des
Year1998
Volume4
Pages381-96
AuthorsRice KD, Tanaka RD, Katz BA, Numerof RP, Moore WR
TitleInhibitors of tryptase for the treatment of mast cell-mediated diseases.
[6]
CommentsX-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
Medline ID98180625
PubMed ID9521329
JournalNature
Year1998
Volume392
Pages306-11
AuthorsPereira PJ, Bergner A, Macedo-Ribeiro S, Huber R, Matschiner G, Fritz H, Sommerhoff CP, Bode W
TitleHuman beta-tryptase is a ring-like tetramer with active sites facing a central pore.
Related PDB1a0l
Related UniProtKBP20231
[7]
PubMed ID9533631
JournalPeptides
Year1998
Volume19
Pages437-43
AuthorsErba F, Fiorucci L, Coletta M, Ascoli F
TitleBovine mast cell tryptase inactivation: effect of temperature.
[8]
PubMed ID10480954
JournalJ Biol Chem
Year1999
Volume274
Pages27331-7
AuthorsWilharm E, Parry MA, Friebel R, Tschesche H, Matschiner G, Sommerhoff CP, Jenne DE
TitleGeneration of catalytically active granzyme K from Escherichia coli inclusion bodies and identification of efficient granzyme K inhibitors in human plasma.
[9]
CommentsX-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS).
Medline ID99432168
PubMed ID10500112
JournalProc Natl Acad Sci U S A
Year1999
Volume96
Pages10984-91
AuthorsSommerhoff CP, Bode W, Pereira PJ, Stubbs MT, Sturzebecher J, Piechottka GP, Matschiner G, Bergner A
TitleThe structure of the human betaII-tryptase tetramer: fo(u)r better or worse.
Related UniProtKBP20231
[10]
PubMed ID10944445
JournalBiochem Biophys Res Commun
Year2000
Volume275
Pages77-83
AuthorsAlm AK, Gagnemo-Persson R, Sorsa T, Sundelin J
TitleExtrapancreatic trypsin-2 cleaves proteinase-activated receptor-2.
[11]
PubMed ID10708866
JournalBiochim Biophys Acta
Year2000
Volume1477
Pages307-23
AuthorsKam CM, Hudig D, Powers JC
TitleGranzymes (lymphocyte serine proteases): characterization with natural and synthetic substrates and inhibitors.
[12]
PubMed ID10708850
JournalBiochim Biophys Acta
Year2000
Volume1477
Pages75-89
AuthorsSommerhoff CP, Bode W, Matschiner G, Bergner A, Fritz H
TitleThe human mast cell tryptase tetramer: a fascinating riddle solved by structure.
[13]
PubMed ID10617625
JournalJ Biol Chem
Year2000
Volume275
Pages351-8
AuthorsHuang C, Morales G, Vagi A, Chanasyk K, Ferrazzi M, Burklow C, Qiu WT, Feyfant E, Sali A, Stevens RL
TitleFormation of enzymatically active, homotypic, and heterotypic tetramers of mouse mast cell tryptases. Dependence on a conserved Trp-rich domain on the surface.
[14]
PubMed ID11734467
JournalAm J Respir Crit Care Med
Year2001
Volume164
PagesS52-8
AuthorsSommerhoff CP
TitleMast cell tryptases and airway remodeling.
[15]
PubMed ID11172730
JournalBiochem Pharmacol
Year2001
Volume61
Pages271-6
AuthorsErba F, Fiorucci L, Pascarella S, Menegatti E, Ascenzi P, Ascoli F
TitleSelective inhibition of human mast cell tryptase by gabexate mesylate, an antiproteinase drug.
[16]
PubMed ID11325588
JournalChem Biol
Year2001
Volume8
Pages313-27
AuthorsSchaschke N, Matschiner G, Zettl F, Marquardt U, Bergner A, Bode W, Sommerhoff CP, Moroder L
TitleBivalent inhibition of human beta-tryptase.
[17]
PubMed ID11602603
JournalJ Biol Chem
Year2001
Volume276
Pages49169-82
AuthorsWong GW, Yasuda S, Madhusudhan MS, Li L, Yang Y, Krilis SA, Sali A, Stevens RL
TitleHuman tryptase epsilon (PRSS22), a new member of the chromosome 16p13.3 family of human serine proteases expressed in airway epithelial cells.
[18]
PubMed ID11060286
JournalJ Biol Chem
Year2001
Volume276
Pages3683-90
AuthorsZhang D, Pasternack MS, Beresford PJ, Wagner L, Greenberg AH, Lieberman J
TitleInduction of rapid histone degradation by the cytotoxic T lymphocyte protease Granzyme A.
[19]
PubMed ID11876641
JournalBiochemistry
Year2002
Volume41
Pages3329-40
AuthorsSelwood T, Wang ZM, McCaslin DR, Schechter NM
TitleDiverse stability and catalytic properties of human tryptase alpha and beta isoforms are mediated by residue differences at the S1 pocket.
[20]
PubMed ID12162961
JournalJ Mol Biol
Year2002
Volume321
Pages491-502
AuthorsMarquardt U, Zettl F, Huber R, Bode W, Sommerhoff C
TitleThe crystal structure of human alpha1-tryptase reveals a blocked substrate-binding region.
[21]
PubMed ID11908961
JournalJ Nat Prod
Year2002
Volume65
Pages259-61
AuthorsMurakami Y, Takei M, Shindo K, Kitazume C, Tanaka J, Higa T, Fukamachi H
TitleCyclotheonamide E4 and E5, new potent tryptase inhibitors from an Ircinia species of sponge.

comments
This enzyme belongs to the peptidase family-S1.
According to the literature [6], this enzyme has got a similar catalytic triad (Ser/His/Asp) to that of trypsin, suggesting a similar mechanism.

createdupdated
2003-10-072011-02-18


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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