KEGG   ENZYME: 3.4.21.1Help
Entry
EC 3.4.21.1                 Enzyme                                 

Name
chymotrypsin;
chymotrypsins A and B;
alpha-chymar ophth;
avazyme;
chymar;
chymotest;
enzeon;
quimar;
quimotrase;
alpha-chymar;
alpha-chymotrypsin A;
alpha-chymotrypsin
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Serine endopeptidases
BRITE hierarchy
Reaction(IUBMB)
Preferential cleavage: Tyr!, Trp!, Phe!, Leu!
Comment
Chymotrypsin A is formed from cattle and pig chymotrypsinogen A, several iso-forms being produced according to the number of bonds hydrolysed in the precursor. Chymotrypsin B (formerly listed as EC 3.4.4.6), formed from chymotrypsinogen B, is homologous with chymotrypsin A. Enzymes with specificity similar to that of chymotrypsins A and B have been isolated from many species. In peptidase family S1 (trypsin family)
History
EC 3.4.21.1 created 1961 as EC 3.4.4.5 and EC 3.4.4.6, transferred 1972 to EC 3.4.21.1
Orthology
K01310  chymotrypsin
Genes
HSA: 1504(CTRB1) 440387(CTRB2)
PTR: 736467(CTRB2) 736783
PPS: 100979112(CTRB2) 100979449(CTRB1)
GGO: 101134917 101141122
PON: 100434840 100447221
NLE: 115836698
MCC: 711100(CTRB2) 713851
MCF: 102146658(CTRB2) 102147021(CTRB1)
CSAB: 103233307 103233308
RRO: 104677837(CTRB2) 104677859
CJC: 100391196(CTRB1) 100401959
MMU: 66473(Ctrb1)
MCAL: 110300407
RNO: 24291(Ctrb1)
MUN: 110554750
CGE: 100769139
NGI: 103725666
HGL: 101710293 101719459(Ctrb1)
CCAN: 109684024(Ctrb2)
TUP: 102489237(CTRB1) 102489643
CFA: 479649 479650(CTRB2) 610373
BTA: 100848132 504241(CTRB1) 618826
SSC: 100621642(CTRB2) 100621820
CFR: 102521639 102521880(CTRB1) 102524246(CTRB2)
DLE: 111179508 111179510(CTRB1)
MYB: 102246722(CTRB1) 102256565
MYD: 102752429(CTRB1)
DRO: 112300682(CTRB1)
PALE: 102897343
LAV: 100672744
MDO: 100023625
GGA: 112529919 431235(CTRB2)
MGP: 100544825
NMEL: 110404411(CTRB1)
APLA: 101790190
ACYG: 106033168
TGU: 100221838
LSR: 110476244
SCAN: 103816662
CCAE: 111944397
FPG: 101924388(CTRB1)
CLV: 102091024
EGZ: 104133960
NNI: 104016383
PADL: 103918119
CMY: 102937055(CTRB1) 102938194
CPIC: 101937265(CTRB1) 101951625
ACS: 100565667(ctrb2)
TSR: 106539016
XLA: 108713630 108715072 379495(ctrl.L) 379607(ctrb1.L) 444360(ctrb2.L)
XTR: 100489516 101733231 394984(ctrb1) 496968(ctrb2) 548358(ctrl)
DRE: 322451(ctrb1) 562139
IPU: 108274430
LCO: 104938940
PRET: 103460505
KMR: 108248653
ALIM: 106532477
POV: 109624876
MALB: 109961663
PKI: 111843547
CIN: 100181838
APLC: 110978230
DME: Dmel_CG18179(CG18179) Dmel_CG6298(Jon74E)
LCQ: 111676828
VEM: 105562761
NVL: 108563252
MYI: 110459661
LAK: 112042437
DGT: 114521678
HMG: 100213885
 » show all
Taxonomy
Reference
1
  Authors
Wilcox, P.E.
  Title
Chymotrypsinogens - chymotrypsins.
  Journal
Methods Enzymol 19:64-108 (1970)
Reference
2
  Authors
Blow, D.M.
  Title
Structure and mechanism of chymotrypsin.
  Journal
Acc Chem Res 9:145-152 (1976)
Reference
3  [PMID:6768556]
  Authors
Bauer CA.
  Title
Active centers of alpha-chymotrypsin and of Streptomyces griseus proteases 1 and 3. S2-P2 enzyme-substrate interactions.
  Journal
Eur J Biochem 105:565-70 (1980)
DOI:10.1111/j.1432-1033.1980.tb04533.x
Reference
4
  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
5  [PMID:2917002]
  Authors
Tomita N, Izumoto Y, Horii A, Doi S, Yokouchi H, Ogawa M, Mori T, Matsubara K.
  Title
Molecular cloning and nucleotide sequence of human pancreatic prechymotrypsinogen cDNA.
  Journal
Biochem Biophys Res Commun 158:569-75 (1989)
DOI:10.1016/S0006-291X(89)80087-7
  Sequence
[hsa:440387 1504]
Other DBs
ExplorEnz - The Enzyme Database: 3.4.21.1
IUBMB Enzyme Nomenclature: 3.4.21.1
ExPASy - ENZYME nomenclature database: 3.4.21.1
BRENDA, the Enzyme Database: 3.4.21.1
CAS: 9004-07-3

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