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: 100615529(PRSS2) 742453 747006(PRSS3)
PPS: 100991392(PRSS2) 100992428 100993013 100993827 100995726(PRSS3)
GGO: 101128494 101145449 101146899(PRSS3) 101147134 101147499 109023093
PON: 100431404(PRSS3) 100443026 100443647 100444247 100456382
NLE: 100591545 100591887(PRSS2) 100592228 100592562
MCC: 698352(PRSS2) 698729(PRSS1) 716882
MCF: 101866288(PRSS2) 102126989 102127372 102128919 102129300 102129692 102130590 102132890
CSAB: 103227060(PRSS2) 103227061 103227062 103227063 103227064 103227334 103227335 103247594 103247596
RRO: 104655097 104674905(PRSS2) 104675858 104675859 104675860 104675862
CJC: 100395240(PRSS2) 100396682
MMU: 100040233(Gm10334) 103964(Try5) 22072(Prss2) 22074(Try4) 436522(Try10) 67373(2210010C04Rik) 73626(1810009J06Rik)
RNO: 103690254(Try5) 24691(Prss1) 25052(Prss2) 286911(Prss3) 286960(Try4) 312273(Tryx4) 362347(Try4) 683849
TUP: 102497899 102498709(PRSS2)
CFA: 100686744(PRSS2) 475521
ORO: 101378334 101380457(PRSS2)
BTA: 282603(PRSS2) 615026(PRSS1) 780933
SSC: 100302368 100525899(PRSS2)
MYD: 102768314
PALE: 102897268
APLA: 101792988(trypsin-I)
FCH: 102054848(PRSS3) 102055855
CLV: 102095003
EGZ: 104121713
DRE: 571079(si:dkeyp-93a5.2) 65223(prss1)
SPU: 578844
SKO: 102807251
DME: Dmel_CG12350 Dmel_CG12351(deltaTry) Dmel_CG12385(thetaTry) Dmel_CG12386(etaTry) Dmel_CG12387(zetaTry) Dmel_CG12388 Dmel_CG18211(betaTry) Dmel_CG18444(alphaTry) Dmel_CG18681(epsilonTry) Dmel_CG30028(gammaTry) Dmel_CG30031(CG30031) Dmel_CG33159(CG33159) Dmel_CG33160(CG33160) Dmel_CG7754(iotaTry) Dmel_CG9564(Try29F)
DSI: Dsimw501_GD10792(Dsim_GD10792) Dsimw501_GD10793(Dsim_GD10793) Dsimw501_GD11483(Dsim_GD11483) Dsimw501_GD11903(Dsim_GD11903) Dsimw501_GD13159(Dsim_GD13159) Dsimw501_GD13161(Dsim_GD13161) Dsimw501_GD13342(Dsim_GD13342) Dsimw501_GD13344(Dsim_GD13344) Dsimw501_GD15391(Dsim_GD15391) Dsimw501_GD15392(Dsim_GD15392) Dsimw501_GD17046(Dsim_GD17046) Dsimw501_GD17603(Dsim_GD17603) Dsimw501_GD21711(Dsim_GD21711) Dsimw501_GD22751(Dsim_GD22751) Dsimw501_GD22850(Dsim_GD22850) Dsimw501_GD22852(Dsim_GD22852) Dsimw501_GD23144(Dsim_GD23144) Dsimw501_GD25584(Dsim_GD25584) Dsimw501_GD25907(Dsim_GD25907) Dsimw501_GD25908(Dsim_GD25908) Dsimw501_GD25909(Dsim_GD25909) Dsimw501_GD27117(Dsim_GD27117) Dsimw501_GD28977(Dsim_GD28977) Dsimw501_GD29052(Dsim_GD29052) Dsimw501_GD29555(Dsim_GD29555)
AGA: AgaP_AGAP004770 AgaP_AGAP008290(TRY6_ANOGA) AgaP_AGAP008292(TRY4_ANOGA) AgaP_AGAP008293(TRY7_ANOGA) AgaP_AGAP008294(TRY3_ANOGA) AgaP_AGAP008295(TRY2_ANOGA) AgaP_AGAP008296(TRY1_ANOGA) AgaP_AGAP008861
AEC: 105147660
NVI: 100114837(SP8) 100114919(SP12)
TCA: 100141587 100142283(P124) 103313996(P75) 103315051(P45) 655599(P80) 655678(P76) 658877(P162) 660786(P67) 662758(P23) 664017(Ctlp-5c)
MYI: 110442984
ANI: AN2366.2
PTE: PTT_10235
SPAR: SPRG_20627
BBAT: Bdt_2544
BBW: BDW_09610
BBAC: EP01_09270
BEX: A11Q_2385
SALU: DC74_839
SALL: SAZ_04695
STRE: GZL_08500
 » 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 11:114-122 (1978)
Reference
2
  Authors
Walsh, K.A.
  Title
Trypsinogens and trypsins of various species.
  Journal
Methods Enzymol 19:41-63 (1970)
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 23:6570-5 (1984)
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 163:303-12 (1987)
DOI:10.1111/j.1432-1033.1987.tb10801.x
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 139:1005-13 (1987)
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 18:1631 (1990)
DOI:10.1093/nar/18.6.1631
  Sequence
[hsa:5646]
Other DBs
ExplorEnz - The Enzyme Database: 3.4.21.4
IUBMB Enzyme Nomenclature: 3.4.21.4
ExPASy - ENZYME nomenclature database: 3.4.21.4
BRENDA, the Enzyme Database: 3.4.21.4
CAS: 9002-07-7

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