KEGG   ENZYME: 3.4.21.4Help
Entry
EC 3.4.21.4                 Enzyme                                 

Name
trypsin;
alpha-trypsin;
beta-trypsin;
cocoonase;
parenzyme;
parenzymol;
tryptar;
trypure;
pseudotrypsin;
tryptase;
tripcellim;
sperm receptor hydrolase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Serine endopeptidases
BRITE hierarchy
Reaction(IUBMB)
Preferential cleavage: Arg!, Lys!
Comment
The single polypeptide chain cattle beta-trypsin is formed from trypsinogen by cleavage of one peptide bond. Further peptide bond cleavages produce alpha and other iso-forms. Isolated as multiple cationic and anionic trypsins [5] from the pancreas of many vertebrates and from lower species including crayfish, insects (cocoonase) and microorganisms (Streptomyces griseus) [3]. Type example of peptidase family S1.
History
EC 3.4.21.4 created 1961 as EC 3.4.4.4, transferred 1972 to EC 3.4.21.4
Orthology
K01312  
trypsin
Genes
HSA: 
5644(PRSS1) 5645(PRSS2) 5646(PRSS3)
PTR: 
PPS: 
GGO: 
PON: 
MCC: 
698352(PRSS2) 698729(PRSS1) 698983(PRSS1) 699238(PRSS2) 716882
MCF: 
MMU: 
100040233(Gm10334) 103964(Try5) 22072(Prss2) 22074(Try4) 436522(Try10) 67373(2210010C04Rik) 73626(1810009J06Rik)
RNO: 
100912089 24691(Prss1) 25052(Prss2) 286911(Prss3) 286960(Try4) 362347(Try4) 683849
CGE: 
HGL: 
TUP: 
CFA: 
AML: 
FCA: 
PTG: 
BTA: 
282603(PRSS2) 615026(PRSS1) 780933
BOM: 
PHD: 
CHX: 
OAS: 
SSC: 
CFR: 
BACU: 
LVE: 
ECB: 
MYB: 
MYD: 
PALE: 
MDO: 
SHR: 
OAA: 
GGA: 
396344(PRSS2) 396345(PRSS3)
MGP: 
TGU: 
FAB: 
PHI: 
APLA: 
FPG: 
FCH: 
CLV: 
ASN: 
AMJ: 
PSS: 
CMY: 
ACS: 
PBI: 
XLA: 
379460(MGC64344)
XTR: 
496623 496627(prss2) 496640(try10) 548509(prss1)
DRE: 
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
CMK: 
BFO: 
CIN: 
SPU: 
DME: 
Dmel_CG12350(lambdaTry) Dmel_CG12351(deltaTry) Dmel_CG12385(thetaTry) Dmel_CG12386(etaTry) Dmel_CG12387(zetaTry) Dmel_CG18211(betaTry) Dmel_CG18444(alphaTry) Dmel_CG18681(epsilonTry) Dmel_CG30028(gammaTry) Dmel_CG30031 Dmel_CG7754(iotaTry) Dmel_CG9564(Try29F)
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
AGA: 
AgaP_AGAP008296(TRY1_ANOGA)
AAG: 
CQU: 
AME: 
413645(SP22)
NVI: 
100114919(SP12)
TCA: 
100141587 100142246 100142283(P124) 103313996 655599(P80) 655678(P76) 658877(P162) 660786(P67) 664017(Ctlp-5c)
BMOR: 
PHU: 
NVE: 
TAD: 
MPP: 
FGR: 
NHE: 
TRE: 
MAW: 
MAJ: 
CMT: 
VAL: 
SSL: 
BFU: 
MBE: 
ANI: 
AFV: 
PNO: 
PTE: 
BZE: 
BSC: 
BOR: 
TPS: 
PIF: 
EHX: 
BBA: 
BBAT: 
BBAC: 
BEX: 
SMA: 
SALU: 
 » show all
Taxonomy
Reference
1
  Authors
Huber, R. and Bode, W.
  Title
Structural basis of the activation and action of trypsin.
  Journal
Acc. Chem. Res. 11 (1978) 114-122.
Reference
2
  Authors
Walsh, K.A.
  Title
Trypsinogens and trypsins of various species.
  Journal
Methods Enzymol. 19 (1970) 41-63.
Reference
3  [PMID:6442164]
  Authors
Read RJ, Brayer GD, Jurasek L, James MN.
  Title
Critical evaluation of comparative model building of Streptomyces griseus trypsin.
  Journal
Biochemistry. 23 (1984) 6570-5.
Reference
4  [PMID:3643848]
  Authors
Fiedler F.
  Title
Effects of secondary interactions on the kinetics of peptide and peptide ester hydrolysis by tissue kallikrein and trypsin.
  Journal
Eur. J. Biochem. 163 (1987) 303-12.
Reference
5  [PMID:3112218]
  Authors
Jelinek DF, Lipsky PE.
  Title
Comparative activation requirements of human peripheral blood, spleen, and lymph node B cells.
  Journal
J. Immunol. 139 (1987) 1005-13.
Reference
6
  Authors
Polgar, L.
  Title
Structure and function of serine proteases.
  Journal
In: Neuberger, A. and Brocklehurst, K. (Eds.), New Comprehensive Biochemistry: Hydrolytic Enzymes, vol. 16, Elsevier, Amsterdam, 1987, p. 159-200.
Reference
7  [PMID:2326201]
  Authors
Tani T, Kawashima I, Mita K, Takiguchi Y.
  Title
Nucleotide sequence of the human pancreatic trypsinogen III cDNA.
  Journal
Nucleic. Acids. Res. 18 (1990) 1631.
  Sequence
[hsa:5646]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9002-07-7

DBGET integrated database retrieval system