DB code: D00194

RLCP classification 1.13.30000.10 : Hydrolysis
CATH domain 2.40.10.10 : Thrombin, subunit H Catalytic domain
2.40.10.10 : Thrombin, subunit H Catalytic domain
E.C. 3.4.21.1
CSA 1ca0 1hja
M-CSA 1ca0 1hja
MACiE

CATH domain Related DB codes (homologues)
2.40.10.10 : Thrombin, subunit H M00139 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

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Contains Pfam MEROPS
Q7SIG2 Chymotrypsin-1
EC 3.4.21.1
Chymotrypsin I
Soli C1
None PF00089 (Trypsin)
[Graphical View]
P00766 Chymotrypsinogen A
EC 3.4.21.1
Chymotrypsin A chain A
Chymotrypsin A chain B
Chymotrypsin A chain C
PF00089 (Trypsin)
[Graphical View]
S01.001 (Serine)
P00767 Chymotrypsinogen B
EC 3.4.21.1
Chymotrypsin B chain A
Chymotrypsin B chain B
Chymotrypsin B chain C
PF00089 (Trypsin)
[Graphical View]
S01.152 (Serine)

KEGG enzyme name
chymotrypsin
chymotrypsins A and B
alpha-chymar ophth
avazyme
chymar
chymotest
enzeon
quimar
quimotrase
alpha-chymar
alpha-chymotrypsin A
alpha-chymotrypsin

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q7SIG2 CTR1_SOLIN Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa. Secreted, extracellular space.
P00766 CTRA_BOVIN Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa. Secreted, extracellular space.
P00767 CTRB_BOVIN Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa. Secreted, extracellular space.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C00012 C00241 C00001 C00012 C04245
E.C.
Compound Peptide Amide H2O Peptide Amino acid(Tyr-, Trp-, Phe-, Leu-)
Type peptide/protein amide group H2O peptide/protein amino acids
ChEBI 15377
15377
2645
2645
PubChem 22247451
962
22247451
962
440270
440270
1eq9A01 Unbound Unbound Unbound Unbound Transition-state-analogue:PMS
1eq9B01 Unbound Unbound Unbound Unbound Transition-state-analogue:PMS
1ab9C Unbound Unbound Unbound Unbound Intermediate-bound:TYR_304(chain D)
1acbE01 Bound:LEU_45-ASP_46(chain I) Unbound Unbound Unbound Unbound
1afqC Analogue:DLE-PHE-FBA(chain D) Unbound Unbound Unbound Unbound
1ca0C Analogue:ARG_15-ALA_16(chain D) Unbound Unbound Unbound Unbound
1ca0H Analogue:ARG_15-ALA_16(chain I) Unbound Unbound Unbound Unbound
1cbwC Analogue:LYS_15-ALA_16(chain D) Unbound Unbound Unbound Unbound
1cbwH Analogue:LYS_15-ALA_16(chain I) Unbound Unbound Unbound Unbound
1cgiE01 Bound:TYR_18-GLU_19(chain I) Unbound Unbound Unbound Unbound
1cgjE01 Bound:LEU_18-GLU_19(chain I) Unbound Unbound Unbound Unbound
1chgA01 Unbound Unbound Unbound Unbound Unbound
1choG Bound:LEU_18-GLU_19(chain I) Unbound Unbound Unbound Unbound
1dlkB01 Unbound Unbound Unbound Unbound Transition-state-analogue:GLY-GLY-PCS(chain I)
1dlkD01 Unbound Unbound Unbound Unbound Transition-state-analogue:GLY-GLY-PCS(chain J)
1ex3A01 Unbound Unbound Unbound Unbound Unbound
1gcdA01 Unbound Unbound Unbound Unbound Transition-state-analogue:DEP
1gctA01 Unbound Unbound Unbound Unbound Intermediate-bound:UNK-PRO-GLY-ALA-TYR(chain B)
1gg6C Unbound Unbound Unbound Unbound Transition-state-analogue:APF
1ggdC Unbound Unbound Unbound Unbound Intermediate-bound:FAF
1ghaG Unbound Unbound Bound:PRO-GLY-VAL-TYR(chain P) Unbound Unbound
1ghbE01 Unbound Unbound Analogue:PRO-GLY-ALA(chain P) Unbound Unbound
1gmcG Unbound Unbound Unbound Unbound Intermediate-bound:PRO-GLY-ALA-TYR(chain B)
1gmdG Unbound Unbound Unbound Unbound Transition-state-bound:PRO-GLY-ALA-TYR-ASP(chain B)
1gmhG Unbound Unbound Unbound Unbound Transition-state-analogue:ISP
1hjaC Analogue:LYS_18-GLU_19(chain I) Unbound Unbound Unbound Unbound
1mtnC Analogue:LYS_315-ALA_316(chain D) Unbound Unbound Unbound Unbound
1mtnG Analogue:LYS_315-ALA_316(chain H) Unbound Unbound Unbound Unbound
1vgcC Unbound Unbound Unbound Unbound Transition-state-analogue:V36
2cgaA01 Unbound Unbound Unbound Unbound Unbound
2cgaB01 Unbound Unbound Unbound Unbound Unbound
2chaC Unbound Unbound Unbound Unbound Transition-state-analogue:TOS
2chaG Unbound Unbound Unbound Unbound Transition-state-analogue:TOS
2gchG Unbound Unbound Unbound Unbound Unbound
2gctA01 Unbound Unbound Unbound Unbound Intermediate-bound:UNK-PRO-GLY-ALA-TYR(chain B)
2gmtA01 Unbound Unbound Unbound Unbound Unbound
2vgcC Unbound Unbound Unbound Unbound Intermediate-analogue:V35
3gchA01 Unbound Unbound Unbound Unbound Intermediate-analogue:OAC
3gctG Unbound Unbound Unbound Unbound Intermediate-bound:UNK-PRO-GLY-ALA-TYR(chain B)
3vgcC Unbound Unbound Unbound Unbound Transition-state-analogue:SRB
4chaC Unbound Unbound Unbound Unbound Unbound
4chaG Unbound Unbound Unbound Unbound Unbound
4gchG Unbound Unbound Unbound Unbound Intermediate-analogue:DMC
4vgcC Unbound Unbound Unbound Unbound Intermediate-analogue:SRD
5chaC Unbound Unbound Unbound Unbound Unbound
5chaG Unbound Unbound Unbound Unbound Unbound
5gchG Unbound Unbound Unbound Unbound Unbound
6chaC Unbound Unbound Unbound Unbound Transition-state-analogue:PBA
6chaG Unbound Unbound Unbound Analogue:PBA Unbound
6gchG Unbound Unbound Unbound Unbound Transition-state-analogue:APF
7gchG Unbound Unbound Unbound Unbound Transition-state-analogue:LPF
8gchG Unbound Unbound Bound:GLY-ALA-TRP(chain C) Unbound Unbound
1eq9A02 Unbound Unbound Unbound Unbound Unbound
1eq9B02 Unbound Unbound Unbound Unbound Unbound
1ab9B Unbound Unbound Unbound Unbound Unbound
1acbE02 Unbound Unbound Unbound Unbound Unbound
1afqB Unbound Unbound Unbound Unbound Unbound
1ca0B Unbound Unbound Unbound Unbound Unbound
1ca0G Unbound Unbound Unbound Unbound Unbound
1cbwB Unbound Unbound Unbound Unbound Unbound
1cbwG Unbound Unbound Unbound Unbound Unbound
1cgiE02 Unbound Unbound Unbound Unbound Unbound
1cgjE02 Unbound Unbound Unbound Unbound Unbound
1chgA02 Unbound Unbound Unbound Unbound Unbound
1choF Unbound Unbound Unbound Unbound Unbound
1dlkB02 Unbound Unbound Unbound Unbound Unbound
1dlkD02 Unbound Unbound Unbound Unbound Unbound
1ex3A02 Unbound Unbound Unbound Unbound Unbound
1gcdA02 Unbound Unbound Unbound Unbound Unbound
1gctA02 Unbound Unbound Unbound Unbound Unbound
1gg6B Unbound Unbound Unbound Unbound Unbound
1ggdB Unbound Unbound Unbound Unbound Unbound
1ghaF Unbound Unbound Unbound Unbound Unbound
1ghbE02 Unbound Unbound Unbound Unbound Unbound
1gmcF Unbound Unbound Unbound Unbound Unbound
1gmdF Unbound Unbound Unbound Unbound Unbound
1gmhF Unbound Unbound Unbound Unbound Unbound
1hjaB Unbound Unbound Unbound Unbound Unbound
1mtnB Unbound Unbound Unbound Unbound Unbound
1mtnF Unbound Unbound Unbound Unbound Unbound
1vgcB Unbound Unbound Unbound Unbound Unbound
2cgaA02 Unbound Unbound Unbound Unbound Unbound
2cgaB02 Unbound Unbound Unbound Unbound Unbound
2chaB Unbound Unbound Unbound Unbound Unbound
2chaF Unbound Unbound Unbound Unbound Unbound
2gchF Unbound Unbound Unbound Unbound Unbound
2gctA02 Unbound Unbound Unbound Unbound Unbound
2gmtA02 Unbound Unbound Unbound Unbound Unbound
2vgcB Unbound Unbound Unbound Unbound Unbound
3gchA02 Unbound Unbound Unbound Unbound Unbound
3gctF Unbound Unbound Unbound Unbound Unbound
3vgcB Unbound Unbound Unbound Unbound Unbound
4chaB Unbound Unbound Unbound Unbound Unbound
4chaF Unbound Unbound Unbound Unbound Unbound
4gchF Unbound Unbound Unbound Unbound Unbound
4vgcB Unbound Unbound Unbound Unbound Unbound
5chaB Unbound Unbound Unbound Unbound Unbound
5chaF Unbound Unbound Unbound Unbound Unbound
5gchF Unbound Unbound Unbound Unbound Unbound
6chaB Unbound Unbound Unbound Unbound Unbound
6chaF Unbound Unbound Unbound Unbound Unbound
6gchF Unbound Unbound Unbound Unbound Unbound
7gchF Unbound Unbound Unbound Unbound Unbound
8gchF Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1eq9A01 SER 195 GLY 193;SER 195
1eq9B01 SER 495 GLY 493;SER 495
1ab9C SER 195 GLY 193;SER 195
1acbE01 SER 195 GLY 193;SER 195
1afqC SER 195 GLY 193;SER 195
1ca0C SER 195 GLY 193;SER 195
1ca0H SER 195 GLY 193;SER 195
1cbwC SER 195 GLY 193;SER 195
1cbwH SER 195 GLY 193;SER 195
1cgiE01 SER 195 GLY 193;SER 195
1cgjE01 SER 195 GLY 193;SER 195
1chgA01 SER 195 GLY 193;SER 195
1choG SER 195 GLY 193;SER 195
1dlkB01 SER 195 GLY 193;SER 195
1dlkD01 SER 195 GLY 193;SER 195
1ex3A01 SER 195 GLY 193;SER 195
1gcdA01 SER 195 GLY 193;SER 195
1gctA01 SER 195 GLY 193;SER 195
1gg6C SER 195 GLY 193;SER 195
1ggdC SER 195 GLY 193;SER 195
1ghaG SER 195 GLY 193;SER 195
1ghbE01 SER 195 GLY 193;SER 195
1gmcG SER 195 GLY 193;SER 195
1gmdG SER 195 GLY 193;SER 195
1gmhG SER 195 GLY 193;SER 195
1hjaC SER 195 GLY 193;SER 195
1mtnC SER 195 GLY 193;SER 195
1mtnG SER 195 GLY 193;SER 195
1vgcC SER 195 GLY 193;SER 195
2cgaA01 SER 195 GLY 193;SER 195
2cgaB01 SER 195 GLY 193;SER 195
2chaC SER 195 GLY 193;SER 195
2chaG SER 195 GLY 193;SER 195
2gchG SER 195 GLY 193;SER 195
2gctA01 SER 195 GLY 193;SER 195
2gmtA01 SER 195 GLY 193;SER 195
2vgcC SER 195 GLY 193;SER 195
3gchA01 SER 195 GLY 193;SER 195
3gctG SER 195 GLY 193;SER 195
3vgcC SER 195 GLY 193;SER 195
4chaC SER 195 GLY 193;SER 195
4chaG SER 195 GLY 193;SER 195
4gchG SER 195 GLY 193;SER 195
4vgcC SER 195 GLY 193;SER 195
5chaC SER 195 GLY 193;SER 195
5chaG SER 195 GLY 193;SER 195
5gchG SER 195 GLY 193;SER 195
6chaC SER 195 GLY 193;SER 195
6chaG SER 195 GLY 193;SER 195
6gchG SER 195 GLY 193;SER 195
7gchG SER 195 GLY 193;SER 195
8gchG SER 195 GLY 193;SER 195
1eq9A02 HIS 57;ASP 102
1eq9B02 HIS 357;ASP 402
1ab9B HIS 57;ASP 102
1acbE02 HIS 57;ASP 102
1afqB HIS 57;ASP 102
1ca0B HIS 57;ASP 102
1ca0G HIS 57;ASP 102
1cbwB HIS 57;ASP 102
1cbwG HIS 57;ASP 102
1cgiE02 HIS 57;ASP 102
1cgjE02 HIS 57;ASP 102
1chgA02 HIS 57;ASP 102
1choF HIS 57;ASP 102
1dlkB02 HIS 57;ASP 102
1dlkD02 HIS 57;ASP 102
1ex3A02 HIS 57;ASP 102
1gcdA02 HIS 57;ASP 102
1gctA02 HIS 57;ASP 102
1gg6B HIS 57;ASP 102
1ggdB HIS 57;ASP 102
1ghaF HIS 57;ASP 102
1ghbE02 HIS 57;ASP 102
1gmcF HIS 57;ASP 102
1gmdF HIS 57;ASP 102
1gmhF HIS 57;ASP 102
1hjaB HIS 57;ASP 102
1mtnB HIS 57;ASP 102
1mtnF HIS 57;ASP 102
1vgcB HIS 57;ASP 102
2cgaA02 HIS 57;ASP 102
2cgaB02 HIS 57;ASP 102
2chaB HIS 57;ASP 102
2chaF HIS 57;ASP 102
2gchF HIS 57;ASP 102
2gctA02 HIS 57;ASP 102
2gmtA02 HIS 57;ASP 102
2vgcB HIS 57;ASP 102
3gchA02 HIS 57;ASP 102
3gctF HIS 57;ASP 102
3vgcB HIS 57;ASP 102
4chaB HIS 57;ASP 102
4chaF HIS 57;ASP 102
4gchF HIS 57;ASP 102
4vgcB HIS 57;ASP 102
5chaB HIS 57;ASP 102
5chaF HIS 57;ASP 102
5gchF HIS 57;ASP 102
6chaB HIS 57;ASP 102
6chaF HIS 57;ASP 102
6gchF HIS 57;ASP 102
7gchF HIS 57;ASP 102
8gchF HIS 57;ASP 102

References for Catalytic Mechanism
References Sections No. 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]
Resource
Comments ACTIVE SITE.
Medline ID 67181723
PubMed ID 5971785
Journal Biochem J
Year 1966
Volume 101
Pages 232-41
Authors Smillie LB, Hartley BS
Title Histidine sequences in the active centres of some 'serine' proteinases.
Related PDB
Related UniProtKB P00766
[2]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF CHYMOTRYPSINOGEN.
Medline ID 70177557
PubMed ID 5442169
Journal Biochemistry
Year 1970
Volume 9
Pages 1997-2009
Authors Freer ST, Kraut J, Robertus JD, Wright HT, Xuong NH
Title Chymotrypsinogen: 2.5-angstrom crystal structure, comparison with alpha-chymotrypsin, and implications for zymogen activation.
Related PDB 1chg
Related UniProtKB P00766
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY.
Medline ID 72035052
PubMed ID 4399050
Journal Philos Trans R Soc Lond B Biol Sci
Year 1970
Volume 257
Pages 67-76
Authors Birktoft JJ, Blow DM, Henderson R, Steitz TA
Title I. Serine proteinases. The structure of alpha-chymotrypsin.
Related PDB
Related UniProtKB P00766
[4]
Resource
Comments
Medline ID
PubMed ID 4508173
Journal Cold Spring Harb Symp Quant Biol
Year 1972
Volume 36
Pages 63-70
Authors Henderson R, Wright CS, Hess GP, Blow DM
Title Chymotrypsin: what can we learn about catalysis from xray diffraction?
Related PDB
Related UniProtKB
[5]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 5069789
Journal J Mol Biol
Year 1972
Volume 68
Pages 187-240
Authors Birktoft JJ, Blow DM
Title Structure of crystalline -chymotrypsin. V. The atomic structure of tosyl- -chymotrypsin at 2 A resolution.
Related PDB 2cha
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 4634509
Journal J Mol Biol
Year 1972
Volume 63
Pages 295-303
Authors Wright CS, Hess GP, Blow DM
Title Structure of crystalline methylchymotrypsin.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 4745847
Journal J Mol Biol
Year 1973
Volume 79
Pages 1-11
Authors Wright HT
Title Comparison of the crystal structures of chymotrypsinogenA and alphachymotrypsin.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 4597310
Journal Ann N Y Acad Sci
Year 1974
Volume 227
Pages 438-45
Authors Hartley BS
Title The active centers of serine proteinases.: Review
Related PDB
Related UniProtKB
[9]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF GAMMA-CHYMOTRYPSIN.
Medline ID 82078042
PubMed ID 6914398
Journal J Mol Biol
Year 1981
Volume 148
Pages 449-79
Authors Cohen GH, Silverton EW, Davies DR
Title Refined crystal structure of gamma-chymotrypsin at 1.9 A resolution. Comparison with other pancreatic serine proteases.
Related PDB 2gch
Related UniProtKB P00766
[10]
Resource
Comments
Medline ID
PubMed ID 6750612
Journal Proc Natl Acad Sci U S A
Year 1982
Volume 79
Pages 4868-72
Authors Fujinaga M, Read RJ, Sielecki A, Ardelt W, Laskowski M Jr, James MN
Title Refined crystal structure of the molecular complex of Streptomyces griseus protease B, a serine protease, with the third domain of the ovomucoid inhibitor from turkey.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 3971987
Journal Eur J Biochem
Year 1985
Volume 147
Pages 387-95
Authors Bode W, Epp O, Huber R, Laskowski M Jr, Ardelt W
Title The crystal and molecular structure of the third domain of silver pheasant ovomucoid (OMSVP3).
Related PDB
Related UniProtKB
[12]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 3980476
Journal J Biol Chem
Year 1985
Volume 260
Pages 4264-75
Authors Blevins RA, Tulinsky A
Title The refinement and the structure of the dimer of alpha-chymotrypsin at 1.67-A resolution.
Related PDB 5cha
Related UniProtKB
[13]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF ALPHA-CHYMOTRYPSIN.
Medline ID 86011575
PubMed ID 4046030
Journal J Mol Biol
Year 1985
Volume 184
Pages 703-11
Authors Tsukada H, Blow DM
Title Structure of alpha-chymotrypsin refined at 1.68 A resolution.
Related PDB 4cha
Related UniProtKB P00766
[14]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 4057257
Journal J Mol Biol
Year 1985
Volume 185
Pages 595-624
Authors Wang D, Bode W, Huber R
Title Bovine chymotrypsinogen A X-ray crystal structure analysis and refinement of a new crystal form at 1.8 A resolution.
Related PDB 2cga
Related UniProtKB
[15]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 3584139
Journal J Biol Chem
Year 1987
Volume 262
Pages 7737-43
Authors Tulinsky A, Blevins RA
Title Structure of a tetrahedral transition state complex of alpha-chymotrypsin dimer at 1.8-A resolution.
Related PDB 6cha
Related UniProtKB
[16]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 3477645
Journal J Mol Biol
Year 1987
Volume 195
Pages 397-418
Authors Fujinaga M, Sielecki AR, Read RJ, Ardelt W, Laskowski M Jr, James MN
Title Crystal and molecular structures of the complex of alpha-chymotrypsin with its inhibitor turkey ovomucoid third domain at 1.8 A resolution.
Related PDB 1cho
Related UniProtKB
[17]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 2819046
Journal Biochemistry
Year 1989
Volume 28
Pages 7033-8
Authors Dixon MM, Matthews BW
Title Is gamma-chymotrypsin a tetrapeptide acyl-enzyme adduct of alpha-chymotrypsin?
Related PDB 1gct
Related UniProtKB
[18]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 2271520
Journal Biochemistry
Year 1990
Volume 29
Pages 7600-7
Authors Brady K, Wei AZ, Ringe D, Abeles RH
Title Structure of chymotrypsin-trifluoromethyl ketone inhibitor complexes: comparison of slowly and rapidly equilibrating inhibitors.
Related PDB 6gch 7gch
Related UniProtKB
[19]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 2364065
Journal Biochemistry
Year 1990
Volume 29
Pages 4871-9
Authors Stoddard BL, Bruhnke J, Porter N, Ringe D, Petsko GA
Title Structure and activity of two photoreversible cinnamates bound to chymotrypsin.
Related PDB 4gch
Related UniProtKB
[20]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 2036388
Journal Biochemistry
Year 1991
Volume 30
Pages 5217-25
Authors Harel M, Su CT, Frolow F, Silman I, Sussman JL
Title Gamma-chymotrypsin is a complex of alpha-chymotrypsin with its own autolysis products.
Related PDB 8gch
Related UniProtKB
[21]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 1888717
Journal Int J Biol Macromol
Year 1991
Volume 13
Pages 89-96
Authors Dixon MM, Brennan RG, Matthews BW
Title Structure 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 PDB 2gct 3gct
Related UniProtKB
[22]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 1942036
Journal J Mol Biol
Year 1991
Volume 221
Pages 909-18
Authors Harel M, Su CT, Frolow F, Ashani Y, Silman I, Sussman JL
Title Refined crystal structures of "aged" and "non-aged" organophosphoryl conjugates of gamma-chymotrypsin.
Related PDB 1gcd 1gmh
Related UniProtKB
[23]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 1870127
Journal J Mol Biol
Year 1991
Volume 220
Pages 711-22
Authors Hecht HJ, Szardenings M, Collins J, Schomburg D
Title Three-dimensional structure of the complexes between bovine chymotrypsinogen A and two recombinant variants of human pancreatic secretory trypsin inhibitor (Kazal-type).
Related PDB 1cgi 1cgj
Related UniProtKB
[24]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 1583684
Journal J Mol Biol
Year 1992
Volume 225
Pages 107-23
Authors Frigerio F, Coda A, Pugliese L, Lionetti C, Menegatti E, Amiconi G, Schnebli HP, Ascenzi P, Bolognesi M
Title Crystal and molecular structure of the bovine alpha-chymotrypsin-eglin c complex at 2.0 A resolution.
Related PDB 1acb
Related UniProtKB
[25]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 7947790
Journal Biochemistry
Year 1994
Volume 33
Pages 13792-800
Authors Kreutter K, Steinmetz AC, Liang TC, Prorok M, Abeles RH, Ringe D
Title Three-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 PDB 2gmt
Related UniProtKB
[26]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 8003497
Journal Biochemistry
Year 1994
Volume 33
Pages 7326-36
Authors Yennawar NH, Yennawar HP, Farber GK
Title X-ray crystal structure of gamma-chymotrypsin in hexane.
Related PDB 1ab9 1afq 1gmc 1gmd
Related UniProtKB
[27]
Resource
Comments
Medline ID
PubMed ID 8089842
Journal J Mol Biol
Year 1994
Volume 242
Pages 203-14
Authors Krezel AM, Darba P, Robertson AD, Fejzo J, Macura S, Markley JL
Title Solution structure of turkey ovomucoid third domain as determined from nuclear magnetic resonance data.
Related PDB
Related UniProtKB
[28]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID
Journal J Am Chem Soc
Year 1995
Volume 117
Pages 577-85
Authors Yennawar HP, Yennawar NH, Farber GK
Title A structural explanation for enzyme memory in nonaqueous solvents.
Related PDB 1gha 1ghb
Related UniProtKB
[29]
Resource
Comments
Medline ID
PubMed ID 8642605
Journal J Mol Biol
Year 1996
Volume 258
Pages 501-37
Authors Lesk AM, Fordham WD
Title Conservation and variability in the structures of serine proteinases of the chymotrypsin family.
Related PDB
Related UniProtKB
[30]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 9179777
Journal J Mol Recognit
Year 1997
Volume 10
Pages 26-35
Authors Capasso C, Rizzi M, Menegatti E, Ascenzi P, Bolognesi M
Title Crystal structure of the bovine alpha-chymotrypsin:Kunitz inhibitor complex. An example of multiple protein:protein recognition sites.
Related PDB 1mtn
Related UniProtKB
[31]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 9300481
Journal Protein Sci
Year 1997
Volume 6
Pages 1806-24
Authors Scheidig AJ, Hynes TR, Pelletier LA, Wells JA, Kossiakoff AA
Title Crystal 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 PDB 1ca0 1cbw
Related UniProtKB
[32]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 9425066
Journal Biochemistry
Year 1998
Volume 37
Pages 451-62
Authors Stoll VS, Eger BT, Hynes RC, Martichonok V, Jones JB, Pai EF
Title Differences in binding modes of enantiomers of 1-acetamido boronic acid based protease inhibitors: crystal structures of gamma-chymotrypsin and subtilisin Carlsberg complexes.
Related PDB 1vgc 2vgc 3vgc 4vgc
Related UniProtKB
[33]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10713514
Journal Acta Crystallogr D Biol Crystallogr
Year 2000
Volume 56
Pages 280-6
Authors Mac Sweeney A, Birrane G, Walsh MA, O'Connell T, Malthouse JP, Higgins TM
Title Crystal structure of delta-chymotrypsin bound to a peptidyl chloromethyl ketone inhibitor.
Related PDB 1dlk
Related UniProtKB
[34]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10801356
Journal J Mol Biol
Year 2000
Volume 298
Pages 895-901
Authors Botos I, Meyer E, Nguyen M, Swanson SM, Koomen JM, Russell DH, Meyer EF
Title The structure of an insect chymotrypsin.
Related PDB 1eq9
Related UniProtKB
[35]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10873462
Journal J Mol Biol
Year 2000
Volume 300
Pages 235-9
Authors Pjura PE, Lenhoff AM, Leonard SA, Gittis AG
Title Protein crystallization by design: chymotrypsinogen without precipitants.
Related PDB 1ex3
Related UniProtKB
[36]
Resource
Comments
Medline ID
PubMed ID 11327865
Journal Biochemistry
Year 2001
Volume 40
Pages 2439-47
Authors Neidhart D, Wei Y, Cassidy C, Lin J, Cleland WW, Frey PA
Title Correlation of low-barrier hydrogen bonding and oxyanion binding in transition state analogue complexes of chymotrypsin.
Related PDB 1gg6 1ggd
Related UniProtKB
[37]
Resource
Comments
Medline ID
PubMed ID 11258883
Journal Biochemistry
Year 2001
Volume 40
Pages 2723-31
Authors Pan Y, Daggett V
Title Direct 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.
Related PDB
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[38]
Resource
Comments
Medline ID
PubMed ID 11733020
Journal Eur J Biochem
Year 2001
Volume 268
Pages 6238-46
Authors Bodi A, Kaslik G, Venekei I, Graf L
Title Structural determinants of the half-life and cleavage site preference in the autolytic inactivation of chymotrypsin.
Related PDB
Related UniProtKB
[39]
Resource
Comments
Medline ID
PubMed ID 11562364
Journal J Biol Chem
Year 2001
Volume 276
Pages 45079-87
Authors Chen C, Hsu CH, Su NY, Lin YC, Chiou SH, Wu SH
Title Solution structure of a Kunitz-type chymotrypsin inhibitor isolated from the elapid snake Bungarus fasciatus.
Related PDB
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[40]
Resource
Comments
Medline ID
PubMed ID 11495915
Journal J Biol Chem
Year 2001
Volume 276
Pages 38893-8
Authors Roussel A, Mathieu M, Dobbs A, Luu B, Cambillau C, Kellenberger C
Title Complexation of two proteic insect inhibitors to the active site of chymotrypsin suggests decoupled roles for binding and selectivity.
Related PDB
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[41]
Resource
Comments
Medline ID
PubMed ID 11846564
Journal J Mol Biol
Year 2001
Volume 314
Pages 519-25
Authors Ghani U, Ng KK, Atta-ur-Rahman, Choudhary MI, Ullah N, James MN
Title Crystal structure of gamma-chymotrypsin in complex with 7-hydroxycoumarin.
Related PDB
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[42]
Resource
Comments
Medline ID
PubMed ID 11391787
Journal J Mol Recognit
Year 2001
Volume 14
Pages 166-71
Authors Song J, Markley JL
Title NMR 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).
Related PDB
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[43]
Resource
Comments
Medline ID
PubMed ID 12054616
Journal Biochem Biophys Res Commun
Year 2002
Volume 293
Pages 416-20
Authors Simon LM, Kotorman M, Garab G, Laczko I
Title Effects of polyhydroxy compounds on the structure and activity of alpha-chymotrypsin.
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[44]
Resource
Comments
Medline ID
PubMed ID 11909728
Journal Bioorg Med Chem Lett
Year 2002
Volume 12
Pages 1109-12
Authors Wouters J, Huygens M, Pochet L, Pirotte B, Durant F, Masereel B
Title Structural approach of the mechanism of inhibition of alpha-chymotrypsin by coumarins.
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[45]
Resource
Comments
Medline ID
PubMed ID 12209825
Journal Biotechnol Bioeng
Year 2002
Volume 79
Pages 539-49
Authors Clark DS, Bailey JE
Title Structure-function relationships in immobilized chymotrypsin catalysis.
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[46]
Resource
Comments
Medline ID
PubMed ID 11960433
Journal J Am Chem Soc
Year 2002
Volume 124
Pages 4196-7
Authors Westler WM, Frey PA, Lin J, Wemmer DE, Morimoto H, Williams PG, Markley JL
Title Evidence for a strong hydrogen bond in the catalytic dyad of transition-state analogue inhibitor complexes of chymotrypsin from proton-triton NMR isotope shifts.
Related PDB
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[47]
Resource
Comments
Medline ID
PubMed ID 12452711
Journal J Am Chem Soc
Year 2002
Volume 124
Pages 14373-81
Authors Westler WM, Weinhold F, Markley JL
Title Quantum chemical calculations on structural models of the catalytic site of chymotrypsin: comparison of calculated results with experimental data from NMR spectroscopy.
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[48]
Resource
Comments
Medline ID
PubMed ID 12015318
Journal J Biol Chem
Year 2002
Volume 277
Pages 28031-7
Authors Kolodziej SJ, Wagenknecht T, Strickland DK, Stoops JK
Title The three-dimensional structure of the human alpha 2-macroglobulin dimer reveals its structural organization in the tetrameric native and chymotrypsin alpha 2-macroglobulin complexes.
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[49]
Resource
Comments
Medline ID
PubMed ID 12427971
Journal Proc Natl Acad Sci U S A
Year 2002
Volume 99
Pages 15297-302
Authors Pal SK, Peon J, Zewail AH
Title Ultrafast surface hydration dynamics and expression of protein functionality: alpha -Chymotrypsin.
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[50]
Resource
Comments
Medline ID
PubMed ID 12705877
Journal Biochem Biophys Res Commun
Year 2003
Volume 304
Pages 18-21
Authors Kotorman M, Laczko I, Szabo A, Simon LM
Title Effects of Ca2+ on catalytic activity and conformation of trypsin and alpha-chymotrypsin in aqueous ethanol.
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[51]
Resource
Comments
Medline ID
PubMed ID 12589768
Journal J Mol Biol
Year 2003
Volume 326
Pages 1271-88
Authors Filfil R, Chalikian TV
Title The 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.
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[52]
Resource
Comments
Medline ID
PubMed ID 14568540
Journal J Mol Biol
Year 2003
Volume 333
Pages 845-61
Authors Helland R, Czapinska H, Leiros I, Olufsen M, Otlewski J, Smalas AO
Title Structural consequences of accommodation of four non-cognate amino acid residues in the S1 pocket of bovine trypsin and chymotrypsin.
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[53]
Resource
Comments
Medline ID
PubMed ID 12927546
Journal J Mol Biol
Year 2003
Volume 331
Pages 1121-30
Authors Szabo E, Venekei I, Bocskei Z, Naray-Szabo G, Graf L
Title Three 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.
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[54]
Resource
Comments
Medline ID
PubMed ID 14560053
Journal Protein Eng
Year 2003
Volume 16
Pages 673-81
Authors Mucsi Z, Gaspari Z, Orosz G, Perczel A
Title Structure-oriented rational design of chymotrypsin inhibitor models.
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[55]
Resource
Comments
Medline ID
PubMed ID 14730979
Journal Biochemistry
Year 2004
Volume 43
Pages 742-7
Authors Hengge AC, Stein RL
Title Role of protein conformational mobility in enzyme catalysis: acylation of alpha-chymotrypsin by specific peptide substrates.
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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.

Created Updated
2004-10-14 2009-03-30