EzCatDB: D00194

DB codeD00194
RLCP classification1.13.30000.10
CATH domainDomain 12.40.10.10Catalytic domain
Domain 22.40.10.10Catalytic domain
E.C.3.4.21.1
CSA1ca0,1hja

CATH domainRelated DB codes (homologues)
2.40.10.10M00139,D00214,M00167,D00426,M00133,D00428,D00429,D00430,D00431,D00432,D00433,D00434,D00435,M00227,M00209,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
Swiss-protKEGG

Q7SIG2P00766P00767
Protein nameChymotrypsin-1Chymotrypsinogen AChymotrypsinogen Bchymotrypsin
chymotrypsins A and B
alpha-chymar ophth
avazyme
chymar
chymotest
enzeon
quimar
quimotrase
alpha-chymar
alpha-chymotrypsin A
alpha-chymotrypsin
SynonymsEC 3.4.21.1
Chymotrypsin I
Soli C1
EC 3.4.21.1
EC 3.4.21.1
ContainsNoneChymotrypsin A chain A
Chymotrypsin A chain B
Chymotrypsin A chain C
Chymotrypsin B chain A
Chymotrypsin B chain B
Chymotrypsin B chain C


Swiss-prot:Accession NumberQ7SIG2P00766P00767
Entry nameCTR1_SOLINCTRA_BOVINCTRB_BOVIN
ActivityPreferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
Subunit


Subcellular locationSecreted, extracellular space.Secreted, extracellular space.Secreted, extracellular space.
Cofactor




SubstratesProductsintermediates
KEGG-idC00012C00241C00001C00012C04245
CompoundPeptideAmideH2OPeptideAmino acid(Tyr-, Trp-, Phe-, Leu-)
Typepeptide/proteinamide groupH2Opeptide/proteinamino acids
1eq9A01UnboundUnbound
UnboundUnboundTransition-state-analogue:PMS
1eq9B01UnboundUnbound
UnboundUnboundTransition-state-analogue:PMS
1ab9CUnboundUnbound
UnboundUnboundIntermediate-bound:TYR 304(chain D)
1acbE01Bound:LEU 45-ASP 46(chain I)Unbound
UnboundUnboundUnbound
1afqCAnalogue:DLE-PHE-FBA(chain D)Unbound
UnboundUnboundUnbound
1ca0CAnalogue:ARG 15-ALA 16(chain D)Unbound
UnboundUnboundUnbound
1ca0HAnalogue:ARG 15-ALA 16(chain I)Unbound
UnboundUnboundUnbound
1cbwCAnalogue:LYS 15-ALA 16(chain D)Unbound
UnboundUnboundUnbound
1cbwHAnalogue:LYS 15-ALA 16(chain I)Unbound
UnboundUnboundUnbound
1cgiE01Bound:TYR 18-GLU 19(chain I)Unbound
UnboundUnboundUnbound
1cgjE01Bound:LEU 18-GLU 19(chain I)Unbound
UnboundUnboundUnbound
1chgA01UnboundUnbound
UnboundUnboundUnbound
1choGBound:LEU 18-GLU 19(chain I)Unbound
UnboundUnboundUnbound
1dlkB01UnboundUnbound
UnboundUnboundTransition-state-analogue:GLY-GLY-PCS(chain I)
1dlkD01UnboundUnbound
UnboundUnboundTransition-state-analogue:GLY-GLY-PCS(chain J)
1ex3A01UnboundUnbound
UnboundUnboundUnbound
1gcdA01UnboundUnbound
UnboundUnboundTransition-state-analogue:DEP
1gctA01UnboundUnbound
UnboundUnboundIntermediate-bound:UNK-PRO-GLY-ALA-TYR(chain B)
1gg6CUnboundUnbound
UnboundUnboundTransition-state-analogue:APF
1ggdCUnboundUnbound
UnboundUnboundIntermediate-bound:FAF
1ghaGUnboundUnbound
Bound:PRO-GLY-VAL-TYR(chain P)UnboundUnbound
1ghbE01UnboundUnbound
Analogue:PRO-GLY-ALA(chain P)UnboundUnbound
1gmcGUnboundUnbound
UnboundUnboundIntermediate-bound:PRO-GLY-ALA-TYR(chain B)
1gmdGUnboundUnbound
UnboundUnboundTransition-state-bound:PRO-GLY-ALA-TYR-ASP(chain B)
1gmhGUnboundUnbound
UnboundUnboundTransition-state-analogue:ISP
1hjaCAnalogue:LYS 18-GLU 19(chain I)Unbound
UnboundUnboundUnbound
1mtnCAnalogue:LYS 315-ALA 316(chain D)Unbound
UnboundUnboundUnbound
1mtnGAnalogue:LYS 315-ALA 316(chain H)Unbound
UnboundUnboundUnbound
1vgcCUnboundUnbound
UnboundUnboundTransition-state-analogue:V36
2cgaA01UnboundUnbound
UnboundUnboundUnbound
2cgaB01UnboundUnbound
UnboundUnboundUnbound
2chaCUnboundUnbound
UnboundUnboundTransition-state-analogue:TOS
2chaGUnboundUnbound
UnboundUnboundTransition-state-analogue:TOS
2gchGUnboundUnbound
UnboundUnboundUnbound
2gctA01UnboundUnbound
UnboundUnboundIntermediate-bound:UNK-PRO-GLY-ALA-TYR(chain B)
2gmtA01UnboundUnbound
UnboundUnboundUnbound
2vgcCUnboundUnbound
UnboundUnboundIntermediate-analogue:V35
3gchA01UnboundUnbound
UnboundUnboundIntermediate-analogue:OAC
3gctGUnboundUnbound
UnboundUnboundIntermediate-bound:UNK-PRO-GLY-ALA-TYR(chain B)
3vgcCUnboundUnbound
UnboundUnboundTransition-state-analogue:SRB
4chaCUnboundUnbound
UnboundUnboundUnbound
4chaGUnboundUnbound
UnboundUnboundUnbound
4gchGUnboundUnbound
UnboundUnboundIntermediate-analogue:DMC
4vgcCUnboundUnbound
UnboundUnboundIntermediate-analogue:SRD
5chaCUnboundUnbound
UnboundUnboundUnbound
5chaGUnboundUnbound
UnboundUnboundUnbound
5gchGUnboundUnbound
UnboundUnboundUnbound
6chaCUnboundUnbound
UnboundUnboundTransition-state-analogue:PBA
6chaGUnboundUnbound
UnboundAnalogue:PBAUnbound
6gchGUnboundUnbound
UnboundUnboundTransition-state-analogue:APF
7gchGUnboundUnbound
UnboundUnboundTransition-state-analogue:LPF
8gchGUnboundUnbound
Bound:GLY-ALA-TRP(chain C)UnboundUnbound
1eq9A02UnboundUnbound
UnboundUnboundUnbound
1eq9B02UnboundUnbound
UnboundUnboundUnbound
1ab9BUnboundUnbound
UnboundUnboundUnbound
1acbE02UnboundUnbound
UnboundUnboundUnbound
1afqBUnboundUnbound
UnboundUnboundUnbound
1ca0BUnboundUnbound
UnboundUnboundUnbound
1ca0GUnboundUnbound
UnboundUnboundUnbound
1cbwBUnboundUnbound
UnboundUnboundUnbound
1cbwGUnboundUnbound
UnboundUnboundUnbound
1cgiE02UnboundUnbound
UnboundUnboundUnbound
1cgjE02UnboundUnbound
UnboundUnboundUnbound
1chgA02UnboundUnbound
UnboundUnboundUnbound
1choFUnboundUnbound
UnboundUnboundUnbound
1dlkB02UnboundUnbound
UnboundUnboundUnbound
1dlkD02UnboundUnbound
UnboundUnboundUnbound
1ex3A02UnboundUnbound
UnboundUnboundUnbound
1gcdA02UnboundUnbound
UnboundUnboundUnbound
1gctA02UnboundUnbound
UnboundUnboundUnbound
1gg6BUnboundUnbound
UnboundUnboundUnbound
1ggdBUnboundUnbound
UnboundUnboundUnbound
1ghaFUnboundUnbound
UnboundUnboundUnbound
1ghbE02UnboundUnbound
UnboundUnboundUnbound
1gmcFUnboundUnbound
UnboundUnboundUnbound
1gmdFUnboundUnbound
UnboundUnboundUnbound
1gmhFUnboundUnbound
UnboundUnboundUnbound
1hjaBUnboundUnbound
UnboundUnboundUnbound
1mtnBUnboundUnbound
UnboundUnboundUnbound
1mtnFUnboundUnbound
UnboundUnboundUnbound
1vgcBUnboundUnbound
UnboundUnboundUnbound
2cgaA02UnboundUnbound
UnboundUnboundUnbound
2cgaB02UnboundUnbound
UnboundUnboundUnbound
2chaBUnboundUnbound
UnboundUnboundUnbound
2chaFUnboundUnbound
UnboundUnboundUnbound
2gchFUnboundUnbound
UnboundUnboundUnbound
2gctA02UnboundUnbound
UnboundUnboundUnbound
2gmtA02UnboundUnbound
UnboundUnboundUnbound
2vgcBUnboundUnbound
UnboundUnboundUnbound
3gchA02UnboundUnbound
UnboundUnboundUnbound
3gctFUnboundUnbound
UnboundUnboundUnbound
3vgcBUnboundUnbound
UnboundUnboundUnbound
4chaBUnboundUnbound
UnboundUnboundUnbound
4chaFUnboundUnbound
UnboundUnboundUnbound
4gchFUnboundUnbound
UnboundUnboundUnbound
4vgcBUnboundUnbound
UnboundUnboundUnbound
5chaBUnboundUnbound
UnboundUnboundUnbound
5chaFUnboundUnbound
UnboundUnboundUnbound
5gchFUnboundUnbound
UnboundUnboundUnbound
6chaBUnboundUnbound
UnboundUnboundUnbound
6chaFUnboundUnbound
UnboundUnboundUnbound
6gchFUnboundUnbound
UnboundUnboundUnbound
7gchFUnboundUnbound
UnboundUnboundUnbound
8gchFUnboundUnbound
UnboundUnboundUnbound

Active-site residues
pdbCatalytic residuesMain-chain involved in catalysis
1eq9A01SER 195
GLY 193;SER 195
1eq9B01SER 495
GLY 493;SER 495
1ab9CSER 195
GLY 193;SER 195
1acbE01SER 195
GLY 193;SER 195
1afqCSER 195
GLY 193;SER 195
1ca0CSER 195
GLY 193;SER 195
1ca0HSER 195
GLY 193;SER 195
1cbwCSER 195
GLY 193;SER 195
1cbwHSER 195
GLY 193;SER 195
1cgiE01SER 195
GLY 193;SER 195
1cgjE01SER 195
GLY 193;SER 195
1chgA01SER 195
GLY 193;SER 195
1choGSER 195
GLY 193;SER 195
1dlkB01SER 195
GLY 193;SER 195
1dlkD01SER 195
GLY 193;SER 195
1ex3A01SER 195
GLY 193;SER 195
1gcdA01SER 195
GLY 193;SER 195
1gctA01SER 195
GLY 193;SER 195
1gg6CSER 195
GLY 193;SER 195
1ggdCSER 195
GLY 193;SER 195
1ghaGSER 195
GLY 193;SER 195
1ghbE01SER 195
GLY 193;SER 195
1gmcGSER 195
GLY 193;SER 195
1gmdGSER 195
GLY 193;SER 195
1gmhGSER 195
GLY 193;SER 195
1hjaCSER 195
GLY 193;SER 195
1mtnCSER 195
GLY 193;SER 195
1mtnGSER 195
GLY 193;SER 195
1vgcCSER 195
GLY 193;SER 195
2cgaA01SER 195
GLY 193;SER 195
2cgaB01SER 195
GLY 193;SER 195
2chaCSER 195
GLY 193;SER 195
2chaGSER 195
GLY 193;SER 195
2gchGSER 195
GLY 193;SER 195
2gctA01SER 195
GLY 193;SER 195
2gmtA01SER 195
GLY 193;SER 195
2vgcCSER 195
GLY 193;SER 195
3gchA01SER 195
GLY 193;SER 195
3gctGSER 195
GLY 193;SER 195
3vgcCSER 195
GLY 193;SER 195
4chaCSER 195
GLY 193;SER 195
4chaGSER 195
GLY 193;SER 195
4gchGSER 195
GLY 193;SER 195
4vgcCSER 195
GLY 193;SER 195
5chaCSER 195
GLY 193;SER 195
5chaGSER 195
GLY 193;SER 195
5gchGSER 195
GLY 193;SER 195
6chaCSER 195
GLY 193;SER 195
6chaGSER 195
GLY 193;SER 195
6gchGSER 195
GLY 193;SER 195
7gchGSER 195
GLY 193;SER 195
8gchGSER 195
GLY 193;SER 195
1eq9A02HIS  57;ASP 102

1eq9B02HIS 357;ASP 402

1ab9BHIS  57;ASP 102

1acbE02HIS  57;ASP 102

1afqBHIS  57;ASP 102

1ca0BHIS  57;ASP 102

1ca0GHIS  57;ASP 102

1cbwBHIS  57;ASP 102

1cbwGHIS  57;ASP 102

1cgiE02HIS  57;ASP 102

1cgjE02HIS  57;ASP 102

1chgA02HIS  57;ASP 102

1choFHIS  57;ASP 102

1dlkB02HIS  57;ASP 102

1dlkD02HIS  57;ASP 102

1ex3A02HIS  57;ASP 102

1gcdA02HIS  57;ASP 102

1gctA02HIS  57;ASP 102

1gg6BHIS  57;ASP 102

1ggdBHIS  57;ASP 102

1ghaFHIS  57;ASP 102

1ghbE02HIS  57;ASP 102

1gmcFHIS  57;ASP 102

1gmdFHIS  57;ASP 102

1gmhFHIS  57;ASP 102

1hjaBHIS  57;ASP 102

1mtnBHIS  57;ASP 102

1mtnFHIS  57;ASP 102

1vgcBHIS  57;ASP 102

2cgaA02HIS  57;ASP 102

2cgaB02HIS  57;ASP 102

2chaBHIS  57;ASP 102

2chaFHIS  57;ASP 102

2gchFHIS  57;ASP 102

2gctA02HIS  57;ASP 102

2gmtA02HIS  57;ASP 102

2vgcBHIS  57;ASP 102

3gchA02HIS  57;ASP 102

3gctFHIS  57;ASP 102

3vgcBHIS  57;ASP 102

4chaBHIS  57;ASP 102

4chaFHIS  57;ASP 102

4gchFHIS  57;ASP 102

4vgcBHIS  57;ASP 102

5chaBHIS  57;ASP 102

5chaFHIS  57;ASP 102

5gchFHIS  57;ASP 102

6chaBHIS  57;ASP 102

6chaFHIS  57;ASP 102

6gchFHIS  57;ASP 102

7gchFHIS  57;ASP 102

8gchFHIS  57;ASP 102


References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]Fig.6, p.72-74
[4]Fig.4, p.65-67
[6]p.299-300
[8]Fig.2, p.438-441
[13]p.709-710
[15]

[17]p.7036-7037
[18]p.7606-7607
[25]Scheme 1
[55]Scheme 1

references
[1]
CommentsACTIVE SITE.
Medline ID67181723
PubMed ID5971785
JournalBiochem J
Year1966
Volume101
Pages232-41
AuthorsSmillie LB, Hartley BS
TitleHistidine sequences in the active centres of some 'serine' proteinases.
Related Swiss-protP00766
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF CHYMOTRYPSINOGEN.
Medline ID70177557
PubMed ID5442169
JournalBiochemistry
Year1970
Volume9
Pages1997-2009
AuthorsFreer ST, Kraut J, Robertus JD, Wright HT, Xuong NH
TitleChymotrypsinogen: 2.5-angstrom crystal structure, comparison with alpha-chymotrypsin, and implications for zymogen activation.
Related PDB1chg
Related Swiss-protP00766
[3]
CommentsX-RAY CRYSTALLOGRAPHY.
Medline ID72035052
PubMed ID4399050
JournalPhilos Trans R Soc Lond B Biol Sci
Year1970
Volume257
Pages67-76
AuthorsBirktoft JJ, Blow DM, Henderson R, Steitz TA
TitleI. Serine proteinases. The structure of alpha-chymotrypsin.
Related Swiss-protP00766
[4]
PubMed ID4508173
JournalCold Spring Harb Symp Quant Biol
Year1972
Volume36
Pages63-70
AuthorsHenderson R, Wright CS, Hess GP, Blow DM
TitleChymotrypsin: what can we learn about catalysis from xray diffraction?
[5]
CommentsX-ray crystallography
PubMed ID5069789
JournalJ Mol Biol
Year1972
Volume68
Pages187-240
AuthorsBirktoft JJ, Blow DM
TitleStructure of crystalline -chymotrypsin. V. The atomic structure of tosyl- -chymotrypsin at 2 A resolution.
Related PDB2cha
[6]
PubMed ID4634509
JournalJ Mol Biol
Year1972
Volume63
Pages295-303
AuthorsWright CS, Hess GP, Blow DM
TitleStructure of crystalline methylchymotrypsin.
[7]
PubMed ID4745847
JournalJ Mol Biol
Year1973
Volume79
Pages1-11
AuthorsWright HT
TitleComparison of the crystal structures of chymotrypsinogenA and alphachymotrypsin.
[8]
PubMed ID4597310
JournalAnn N Y Acad Sci
Year1974
Volume227
Pages438-45
AuthorsHartley BS
TitleThe active centers of serine proteinases.: Review
[9]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF GAMMA-CHYMOTRYPSIN.
Medline ID82078042
PubMed ID6914398
JournalJ Mol Biol
Year1981
Volume148
Pages449-79
AuthorsCohen GH, Silverton EW, Davies DR
TitleRefined crystal structure of gamma-chymotrypsin at 1.9 A resolution. Comparison with other pancreatic serine proteases.
Related PDB2gch
Related Swiss-protP00766
[10]
PubMed ID6750612
JournalProc Natl Acad Sci U S A
Year1982
Volume79
Pages4868-72
AuthorsFujinaga M, Read RJ, Sielecki A, Ardelt W, Laskowski M Jr, James MN
TitleRefined crystal structure of the molecular complex of Streptomyces griseus protease B, a serine protease, with the third domain of the ovomucoid inhibitor from turkey.
[11]
PubMed ID3971987
JournalEur J Biochem
Year1985
Volume147
Pages387-95
AuthorsBode W, Epp O, Huber R, Laskowski M Jr, Ardelt W
TitleThe crystal and molecular structure of the third domain of silver pheasant ovomucoid (OMSVP3).
[12]
CommentsX-ray crystallography
PubMed ID3980476
JournalJ Biol Chem
Year1985
Volume260
Pages4264-75
AuthorsBlevins RA, Tulinsky A
TitleThe refinement and the structure of the dimer of alpha-chymotrypsin at 1.67-A resolution.
Related PDB5cha
[13]
CommentsX-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF ALPHA-CHYMOTRYPSIN.
Medline ID86011575
PubMed ID4046030
JournalJ Mol Biol
Year1985
Volume184
Pages703-11
AuthorsTsukada H, Blow DM
TitleStructure of alpha-chymotrypsin refined at 1.68 A resolution.
Related PDB4cha
Related Swiss-protP00766
[14]
CommentsX-ray crystallography
PubMed ID4057257
JournalJ Mol Biol
Year1985
Volume185
Pages595-624
AuthorsWang D, Bode W, Huber R
TitleBovine chymotrypsinogen A X-ray crystal structure analysis and refinement of a new crystal form at 1.8 A resolution.
Related PDB2cga
[15]
CommentsX-ray crystallography
PubMed ID3584139
JournalJ Biol Chem
Year1987
Volume262
Pages7737-43
AuthorsTulinsky A, Blevins RA
TitleStructure of a tetrahedral transition state complex of alpha-chymotrypsin dimer at 1.8-A resolution.
Related PDB6cha
[16]
CommentsX-ray crystallography
PubMed ID3477645
JournalJ Mol Biol
Year1987
Volume195
Pages397-418
AuthorsFujinaga M, Sielecki AR, Read RJ, Ardelt W, Laskowski M Jr, James MN
TitleCrystal and molecular structures of the complex of alpha-chymotrypsin with its inhibitor turkey ovomucoid third domain at 1.8 A resolution.
Related PDB1cho
[17]
CommentsX-ray crystallography
PubMed ID2819046
JournalBiochemistry
Year1989
Volume28
Pages7033-8
AuthorsDixon MM, Matthews BW
TitleIs gamma-chymotrypsin a tetrapeptide acyl-enzyme adduct of alpha-chymotrypsin?
Related PDB1gct
[18]
CommentsX-ray crystallography
PubMed ID2271520
JournalBiochemistry
Year1990
Volume29
Pages7600-7
AuthorsBrady K, Wei AZ, Ringe D, Abeles RH
TitleStructure of chymotrypsin-trifluoromethyl ketone inhibitor complexes: comparison of slowly and rapidly equilibrating inhibitors.
Related PDB6gch,7gch
[19]
CommentsX-ray crystallography
PubMed ID2364065
JournalBiochemistry
Year1990
Volume29
Pages4871-9
AuthorsStoddard BL, Bruhnke J, Porter N, Ringe D, Petsko GA
TitleStructure and activity of two photoreversible cinnamates bound to chymotrypsin.
Related PDB4gch
[20]
CommentsX-ray crystallography
PubMed ID2036388
JournalBiochemistry
Year1991
Volume30
Pages5217-25
AuthorsHarel M, Su CT, Frolow F, Silman I, Sussman JL
TitleGamma-chymotrypsin is a complex of alpha-chymotrypsin with its own autolysis products.
Related PDB8gch
[21]
CommentsX-ray crystallography
PubMed ID1888717
JournalInt J Biol Macromol
Year1991
Volume13
Pages89-96
AuthorsDixon MM, Brennan RG, Matthews BW
TitleStructure of gamma-chymotrypsin in the range pH 2.0 to pH 10.5 suggests that gamma-chymotrypsin is a covalent acyl-enzyme adduct at low pH.
Related PDB2gct,3gct
[22]
CommentsX-ray crystallography
PubMed ID1942036
JournalJ Mol Biol
Year1991
Volume221
Pages909-18
AuthorsHarel M, Su CT, Frolow F, Ashani Y, Silman I, Sussman JL
TitleRefined crystal structures of "aged" and "non-aged" organophosphoryl conjugates of gamma-chymotrypsin.
Related PDB1gcd,1gmh
[23]
CommentsX-ray crystallography
PubMed ID1870127
JournalJ Mol Biol
Year1991
Volume220
Pages711-22
AuthorsHecht HJ, Szardenings M, Collins J, Schomburg D
TitleThree-dimensional structure of the complexes between bovine chymotrypsinogen A and two recombinant variants of human pancreatic secretory trypsin inhibitor (Kazal-type).
Related PDB1cgi,1cgj
[24]
CommentsX-ray crystallography
PubMed ID1583684
JournalJ Mol Biol
Year1992
Volume225
Pages107-23
AuthorsFrigerio F, Coda A, Pugliese L, Lionetti C, Menegatti E, Amiconi G, Schnebli HP, Ascenzi P, Bolognesi M
TitleCrystal and molecular structure of the bovine alpha-chymotrypsin-eglin c complex at 2.0 A resolution.
Related PDB1acb
[25]
CommentsX-ray crystallography
PubMed ID7947790
JournalBiochemistry
Year1994
Volume33
Pages13792-800
AuthorsKreutter K, Steinmetz AC, Liang TC, Prorok M, Abeles RH, Ringe D
TitleThree-dimensional structure of chymotrypsin inactivated with (2S)-N-acetyl-L-alanyl-L-phenylalanyl alpha-chloroethane: implications for the mechanism of inactivation of serine proteases by chloroketones.
Related PDB2gmt
[26]
CommentsX-ray crystallography
PubMed ID8003497
JournalBiochemistry
Year1994
Volume33
Pages7326-36
AuthorsYennawar NH, Yennawar HP, Farber GK
TitleX-ray crystal structure of gamma-chymotrypsin in hexane.
Related PDB1ab9,1afq,1gmc,1gmd
[27]
PubMed ID8089842
JournalJ Mol Biol
Year1994
Volume242
Pages203-14
AuthorsKrezel AM, Darba P, Robertson AD, Fejzo J, Macura S, Markley JL
TitleSolution structure of turkey ovomucoid third domain as determined from nuclear magnetic resonance data.
[28]
CommentsX-ray crystallography
JournalJ Am Chem Soc
Year1995
Volume117
Pages577-85
AuthorsYennawar HP, Yennawar NH, Farber GK
TitleA structural explanation for enzyme memory in nonaqueous solvents.
Related PDB1gha,1ghb
[29]
PubMed ID8642605
JournalJ Mol Biol
Year1996
Volume258
Pages501-37
AuthorsLesk AM, Fordham WD
TitleConservation and variability in the structures of serine proteinases of the chymotrypsin family.
[30]
CommentsX-ray crystallography
PubMed ID9179777
JournalJ Mol Recognit
Year1997
Volume10
Pages26-35
AuthorsCapasso C, Rizzi M, Menegatti E, Ascenzi P, Bolognesi M
TitleCrystal structure of the bovine alpha-chymotrypsin:Kunitz inhibitor complex. An example of multiple protein:protein recognition sites.
Related PDB1mtn
[31]
CommentsX-ray crystallography
PubMed ID9300481
JournalProtein Sci
Year1997
Volume6
Pages1806-24
AuthorsScheidig AJ, Hynes TR, Pelletier LA, Wells JA, Kossiakoff AA
TitleCrystal structures of bovine chymotrypsin and trypsin complexed to the inhibitor domain of Alzheimer's amyloid beta-protein precursor (APPI) and basic pancreatic trypsin inhibitor (BPTI): engineering of inhibitors with altered specificities.
Related PDB1ca0,1cbw
[32]
CommentsX-ray crystallography
PubMed ID9425066
JournalBiochemistry
Year1998
Volume37
Pages451-62
AuthorsStoll VS, Eger BT, Hynes RC, Martichonok V, Jones JB, Pai EF
TitleDifferences in binding modes of enantiomers of 1-acetamido boronic acid based protease inhibitors: crystal structures of gamma-chymotrypsin and subtilisin Carlsberg complexes.
Related PDB1vgc,2vgc,3vgc,4vgc
[33]
CommentsX-ray crystallography
PubMed ID10713514
JournalActa Crystallogr D Biol Crystallogr
Year2000
Volume56
Pages280-6
AuthorsMac Sweeney A, Birrane G, Walsh MA, O'Connell T, Malthouse JP, Higgins TM
TitleCrystal structure of delta-chymotrypsin bound to a peptidyl chloromethyl ketone inhibitor.
Related PDB1dlk
[34]
CommentsX-ray crystallography
PubMed ID10801356
JournalJ Mol Biol
Year2000
Volume298
Pages895-901
AuthorsBotos I, Meyer E, Nguyen M, Swanson SM, Koomen JM, Russell DH, Meyer EF
TitleThe structure of an insect chymotrypsin.
Related PDB1eq9
[35]
CommentsX-ray crystallography
PubMed ID10873462
JournalJ Mol Biol
Year2000
Volume300
Pages235-9
AuthorsPjura PE, Lenhoff AM, Leonard SA, Gittis AG
TitleProtein crystallization by design: chymotrypsinogen without precipitants.
Related PDB1ex3
[36]
PubMed ID11327865
JournalBiochemistry
Year2001
Volume40
Pages2439-47
AuthorsNeidhart D, Wei Y, Cassidy C, Lin J, Cleland WW, Frey PA
TitleCorrelation of low-barrier hydrogen bonding and oxyanion binding in transition state analogue complexes of chymotrypsin.
Related PDB1gg6,1ggd
[37]
PubMed ID11258883
JournalBiochemistry
Year2001
Volume40
Pages2723-31
AuthorsPan Y, Daggett V
TitleDirect comparison of experimental and calculated folding free energies for hydrophobic deletion mutants of chymotrypsin inhibitor 2: free energy perturbation calculations using transition and denatured states from molecular dynamics simulations of unfolding.
[38]
PubMed ID11733020
JournalEur J Biochem
Year2001
Volume268
Pages6238-46
AuthorsBodi A, Kaslik G, Venekei I, Graf L
TitleStructural determinants of the half-life and cleavage site preference in the autolytic inactivation of chymotrypsin.
[39]
PubMed ID11562364
JournalJ Biol Chem
Year2001
Volume276
Pages45079-87
AuthorsChen C, Hsu CH, Su NY, Lin YC, Chiou SH, Wu SH
TitleSolution structure of a Kunitz-type chymotrypsin inhibitor isolated from the elapid snake Bungarus fasciatus.
[40]
PubMed ID11495915
JournalJ Biol Chem
Year2001
Volume276
Pages38893-8
AuthorsRoussel A, Mathieu M, Dobbs A, Luu B, Cambillau C, Kellenberger C
TitleComplexation of two proteic insect inhibitors to the active site of chymotrypsin suggests decoupled roles for binding and selectivity.
[41]
PubMed ID11846564
JournalJ Mol Biol
Year2001
Volume314
Pages519-25
AuthorsGhani U, Ng KK, Atta-ur-Rahman, Choudhary MI, Ullah N, James MN
TitleCrystal structure of gamma-chymotrypsin in complex with 7-hydroxycoumarin.
[42]
PubMed ID11391787
JournalJ Mol Recognit
Year2001
Volume14
Pages166-71
AuthorsSong J, Markley JL
TitleNMR chemical shift mapping of the binding site of a protein proteinase inhibitor: changes in the (1)H, (13)C and (15)N NMR chemical shifts of turkey ovomucoid third domain upon binding to bovine chymotrypsin A(alpha).
[43]
PubMed ID12054616
JournalBiochem Biophys Res Commun
Year2002
Volume293
Pages416-20
AuthorsSimon LM, Kotorman M, Garab G, Laczko I
TitleEffects of polyhydroxy compounds on the structure and activity of alpha-chymotrypsin.
[44]
PubMed ID11909728
JournalBioorg Med Chem Lett
Year2002
Volume12
Pages1109-12
AuthorsWouters J, Huygens M, Pochet L, Pirotte B, Durant F, Masereel B
TitleStructural approach of the mechanism of inhibition of alpha-chymotrypsin by coumarins.
[45]
PubMed ID12209825
JournalBiotechnol Bioeng
Year2002
Volume79
Pages539-49
AuthorsClark DS, Bailey JE
TitleStructure-function relationships in immobilized chymotrypsin catalysis.
[46]
PubMed ID11960433
JournalJ Am Chem Soc
Year2002
Volume124
Pages4196-7
AuthorsWestler WM, Frey PA, Lin J, Wemmer DE, Morimoto H, Williams PG, Markley JL
TitleEvidence for a strong hydrogen bond in the catalytic dyad of transition-state analogue inhibitor complexes of chymotrypsin from proton-triton NMR isotope shifts.
[47]
PubMed ID12452711
JournalJ Am Chem Soc
Year2002
Volume124
Pages14373-81
AuthorsWestler WM, Weinhold F, Markley JL
TitleQuantum chemical calculations on structural models of the catalytic site of chymotrypsin: comparison of calculated results with experimental data from NMR spectroscopy.
[48]
PubMed ID12015318
JournalJ Biol Chem
Year2002
Volume277
Pages28031-7
AuthorsKolodziej SJ, Wagenknecht T, Strickland DK, Stoops JK
TitleThe three-dimensional structure of the human alpha 2-macroglobulin dimer reveals its structural organization in the tetrameric native and chymotrypsin alpha 2-macroglobulin complexes.
[49]
PubMed ID12427971
JournalProc Natl Acad Sci U S A
Year2002
Volume99
Pages15297-302
AuthorsPal SK, Peon J, Zewail AH
TitleUltrafast surface hydration dynamics and expression of protein functionality: alpha -Chymotrypsin.
[50]
PubMed ID12705877
JournalBiochem Biophys Res Commun
Year2003
Volume304
Pages18-21
AuthorsKotorman M, Laczko I, Szabo A, Simon LM
TitleEffects of Ca2+ on catalytic activity and conformation of trypsin and alpha-chymotrypsin in aqueous ethanol.
[51]
PubMed ID12589768
JournalJ Mol Biol
Year2003
Volume326
Pages1271-88
AuthorsFilfil R, Chalikian TV
TitleThe thermodynamics of protein-protein recognition as characterized by a combination of volumetric and calorimetric techniques: the binding of turkey ovomucoid third domain to alpha-chymotrypsin.
[52]
PubMed ID14568540
JournalJ Mol Biol
Year2003
Volume333
Pages845-61
AuthorsHelland R, Czapinska H, Leiros I, Olufsen M, Otlewski J, Smalas AO
TitleStructural consequences of accommodation of four non-cognate amino acid residues in the S1 pocket of bovine trypsin and chymotrypsin.
[53]
PubMed ID12927546
JournalJ Mol Biol
Year2003
Volume331
Pages1121-30
AuthorsSzabo E, Venekei I, Bocskei Z, Naray-Szabo G, Graf L
TitleThree dimensional structures of S189D chymotrypsin and D189S trypsin mutants: the effect of polarity at site 189 on a protease-specific stabilization of the substrate-binding site.
[54]
PubMed ID14560053
JournalProtein Eng
Year2003
Volume16
Pages673-81
AuthorsMucsi Z, Gaspari Z, Orosz G, Perczel A
TitleStructure-oriented rational design of chymotrypsin inhibitor models.
[55]
PubMed ID14730979
JournalBiochemistry
Year2004
Volume43
Pages742-7
AuthorsHengge AC, Stein RL
TitleRole of protein conformational mobility in enzyme catalysis: acylation of alpha-chymotrypsin by specific peptide substrates.

comments
This enzyme belongs to the peptidase family-S1.
This enzyme is one of calssical serine proteases. This enzyme has got a catalytic triad, composed of Ser195/His57/Asp102.
According to the literature, the catalytic reaction proceeds as follows (see D00197):
(1) His57 acts as a general base, by abstracting a proton from the hydroxyl group of Ser195. Here, Asp102 stabilizes the charged His57, and orients the conformation of His57 correctly.
(2) Ser195, whose nucleophilicity can be enhanced by His57, makes a nucleophilic attack on the carbonyl carbon atom of the scissile bond, peptide bond, leading to the formation of a tetrahedral transition-state.
(3) The oxyanion of the transition-state is stabilized by the mainchain amide nitrogens.
(4) His57 acts as a general acid, by protonating to the newly formed amine group. This leads to the dissociation of the first product.
(5) A water molecule makes a nucleophilic attack on the acyl group, resulting in the deacylation.

createdupdated
2004-10-142009-03-30
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 2010)
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)

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