DB code: S00724

RLCP classification 1.12.30000.27 : Hydrolysis
CATH domain 3.40.50.1820 : Rossmann fold Catalytic domain
E.C. 3.1.1.74
CSA 1agy
M-CSA 1agy
MACiE

CATH domain Related DB codes (homologues)
3.40.50.1820 : Rossmann fold S00544 S00344 S00517 S00525 S00526 S00720 S00723 S00725 S00919 S00057 S00374 S00345 S00347 S00348 S00346 S00350 S00352 S00353 S00355 S00356 S00358 D00189 D00210 D00539 T00253

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam RefSeq
P00590 Cutinase 1
EC 3.1.1.74
Cutin hydrolase 1
PF01083 (Cutinase)
[Graphical View]
P11373 Cutinase 1
EC 3.1.1.74
Cutin hydrolase 1
PF01083 (Cutinase)
[Graphical View]
P52956 Cutinase 1
EC 3.1.1.74
Cutin hydrolase 1
L1
PF01083 (Cutinase)
[Graphical View]
XP_001817153.1 (Protein)
XM_001817101.2 (DNA/RNA sequence)

KEGG enzyme name
Cutinase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P00590 CUTI1_FUSSO Cutin + H2O = cutin monomers. Secreted.
P11373 CUTI1_COLGL Cutin + H2O = cutin monomers. Secreted.
P52956 CUTI1_ASPOR Cutin + H2O = cutin monomers. Secreted.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id L00043 C00001 L00068 L00067 L00044 L00069 L00070 L00071 L00072 I00123 I00085 I00086
E.C.
Compound Cutin H2O C16 cutin monomer (Palmitic acid) Hydroxyl-C16 cutin monomer (16-hydroxypalmitic acid) Dihydroxyl-C16 cutin monomer (dihydroxypalmitic acid) C18 cutin monomer (Oleic acid) Hydroxyl-C18 cutin monomer (18-hydroxyoleic acid) Hydroxyl-epoxyl-C18 cutin monomer (9,10-epoxy-18-hydroxystearic acid) Trihydroxyl-C18 cutin monomer (9,10,18-trihydroxystearic acid) Peptidyl-Ser-tetrahedral intermediate (with previous carboxylic-ester) Acyl-enzyme (Peptidyl-Ser-acyl group) Peptidyl-Ser-tetrahedral-intermediate
Type carbohydrate,fatty acid H2O carbohydrate,fatty acid carbohydrate,fatty acid carbohydrate,fatty acid carbohydrate,fatty acid carbohydrate,fatty acid carbohydrate,fatty acid carbohydrate,fatty acid
ChEBI 15377
15377
15756
15756
55328
55328
16196
16196
79312
79312
PubChem 22247451
962
22247451
962
985
985
10466
10466
322588
322588
445639
445639
5312773
5312773
9818312
9818312
5282938
5282938
1agyA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cexA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cuaA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cubA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cucA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cudA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cudB00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cudC00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cueA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cufA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cugA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cuhA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cuiA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cujA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cusA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cuuA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cuvA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cuwA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cuwB00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cuxA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cuyA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cuzA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ffaA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ffbA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ffcA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ffdA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ffeA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1oxmA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:TC4 Unbound Unbound
1oxmB00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:TC4 Unbound Unbound
1xzaA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1xzbA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1xzcA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1xzdA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1xzeA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1xzfA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1xzgA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1xzhA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1xziA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1xzjA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1xzkA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:DFP Unbound Unbound
1xzkB00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:DFP Unbound Unbound
1xzlA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:HEE Unbound Unbound
1xzmA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:DPE Unbound Unbound
2cutA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:DEP Unbound Unbound
3ef3A00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:NXC Unbound Unbound
3esaA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:NXC Unbound Unbound
3esaB00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:NXC Unbound Unbound
3esbA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:NXC Unbound Unbound
3escA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:SXC Unbound Unbound
3esdA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:SXC Unbound Unbound
3dcnA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3dd5A00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:DEP Unbound Unbound
3dd5B00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:DEP Unbound Unbound
3dd5C00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:DEP Unbound Unbound
3dd5D00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:DEP Unbound Unbound
3dd5E00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:DEP Unbound Unbound
3dd5F00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:DEP Unbound Unbound
3dd5G00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:DEP Unbound Unbound
3dd5H00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:DEP Unbound Unbound
3deaA00 Analogue:HZH Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3deaB00 Analogue:HZH Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3gbsA00 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [2], [3], [4], [11], [12], [13], [16], [19]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1agyA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121
1cexA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A
1cuaA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, N172K
1cubA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, N172K, R196D
1cucA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, N172K, R196D
1cudA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, N172K, R196D
1cudB00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, N172K, R196D
1cudC00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, N172K, R196D
1cueA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, Q121L
1cufA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, R156I
1cugA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, R17E, N172K
1cuhA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, R196E
1cuiA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, S120A
1cujA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, S120C
1cusA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A
1cuuA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, A199C
1cuvA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, A85F
1cuwA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, G82A, A85F, V184I, A185L, L189F
1cuwB00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, G82A, A85F, V184I, A185L, L189F
1cuxA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, I114Y
1cuyA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, I189F
1cuzA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, I81G, I182G
1ffaA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant N84A
1ffbA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant N84D
1ffcA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant N84L
1ffdA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant N84W
1ffeA00 ;SER 120;ASP 175;HIS 188 ;GLN 121 mutant S42A
1oxmA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A
1oxmB00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A
1xzaA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, S129C
1xzbA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, S129C
1xzcA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, S129C
1xzdA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, S213C
1xzeA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, S92C
1xzfA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, T144C
1xzgA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, T45A
1xzhA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, T80P
1xziA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, Y119H
1xzjA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, Y38F
1xzkA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A
1xzkB00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A
1xzlA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A
1xzmA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A
2cutA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A
3ef3A00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, N172K
3esaA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, N172K
3esaB00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, N172K
3esbA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, N172K
3escA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, N172K
3esdA00 SER 42;SER 120;ASP 175;HIS 188 SER 42;GLN 121 mutant R32A, N172K
3dcnA00 SER 57;SER 136;ASP 191;HIS 204 SER 57;GLN 137
3dd5A00 SER 57;SER 136;ASP 191;HIS 204 SER 57;GLN 137
3dd5B00 SER 57;SER 136;ASP 191;HIS 204 SER 57;GLN 137
3dd5C00 SER 57;SER 136;ASP 191;HIS 204 SER 57;GLN 137
3dd5D00 SER 57;SER 136;ASP 191;HIS 204 SER 57;GLN 137
3dd5E00 SER 57;SER 136;ASP 191;HIS 204 SER 57;GLN 137
3dd5F00 SER 57;SER 136;ASP 191;HIS 204 SER 57;GLN 137
3dd5G00 SER 57;SER 136;ASP 191;HIS 204 SER 57;GLN 137
3dd5H00 SER 57;SER 136;ASP 191;HIS 204 SER 57;GLN 137
3deaA00 SER 57;SER 136;ASP 191; SER 57;GLN 137 invisible 197-204
3deaB00 SER 57;SER 136;ASP 191; SER 57;GLN 137 invisible 201-204
3gbsA00 SER 48;SER 126;ASP 181;HIS 194 SER 48;GLN 127

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
p.615-618
[3]
p.83, p.86-88
[4]
p.406-409
[11]
p.186-188
[12]
p.90-97
[16]
Fig.1, p.1004-1005
[19]
p.231-233

References
[1]
Resource
Comments
Medline ID
PubMed ID 17779010
Journal Science
Year 1980
Volume 208
Pages 990-1000
Authors Kolattukudy PE
Title Biopolyester membranes of plants: cutin and suberin.
Related PDB
Related UniProtKB
[2]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
Medline ID
PubMed ID 1560844
Journal Nature
Year 1992
Volume 356
Pages 615-8
Authors Martinez C, De Geus P, Lauwereys M, Matthyssens G, Cambillau C
Title Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent.
Related PDB 1cus
Related UniProtKB P00590
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Medline ID
PubMed ID 8286366
Journal Biochemistry
Year 1994
Volume 33
Pages 83-9
Authors Martinez C, Nicolas A, van Tilbeurgh H, Egloff MP, Cudrey C, Verger R, Cambillau C
Title Cutinase, a lipolytic enzyme with a preformed oxyanion hole.
Related PDB 2cut
Related UniProtKB P00590
[4]
Resource
Comments
Medline ID
PubMed ID 8555209
Journal Biochemistry
Year 1996
Volume 35
Pages 398-410
Authors Nicolas A, Egmond M, Verrips CT, de Vlieg J, Longhi S, Cambillau C, Martinez C
Title Contribution of cutinase serine 42 side chain to the stabilization of the oxyanion transition state.
Related PDB 1ffa 1ffb 1ffc 1ffd 1ffe
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 8990497
Journal Proteins
Year 1996
Volume 26
Pages 442-58
Authors Longhi S, Nicolas A, Creveld L, Egmond M, Verrips CT, de Vlieg J, Martinez C, Cambillau C
Title Dynamics of Fusarium solani cutinase investigated through structural comparison among different crystal forms of its variants.
Related PDB 1cua 1cub 1cuc 1cud 1cue 1cuf 1cug 1cuh 1cui 1cuj 1cuu 1cuv 1cuw 1cux 1cuy 1cuz 1xza 1xzd 1xze 1xzf 1xzg 1xzh 1xzi 1xzj 1xzk 1xzl 1xzm
Related UniProtKB
[6]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 17-230.
Medline ID
PubMed ID 9175860
Journal J Mol Biol
Year 1997
Volume 268
Pages 779-99
Authors Longhi S, Czjzek M, Lamzin V, Nicolas A, Cambillau C
Title Atomic resolution (1.0 A) crystal structure of Fusarium solani cutinase: stereochemical analysis.
Related PDB 1agy 1cex
Related UniProtKB P00590
[7]
Resource
Comments
Medline ID
PubMed ID 9041628
Journal Protein Sci
Year 1997
Volume 6
Pages 275-86
Authors Longhi S, Mannesse M, Verheij HM, De Haas GH, Egmond M, Knoops-Mouthuy E, Cambillau C
Title Crystal structure of cutinase covalently inhibited by a triglyceride analogue.
Related PDB 1oxm
Related UniProtKB
[8]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
Medline ID
PubMed ID 9438866
Journal Structure
Year 1997
Volume 5
Pages 1571-84
Authors Kim KK, Song HK, Shin DH, Hwang KY, Choe S, Yoo OJ, Suh SW
Title Crystal structure of carboxylesterase from Pseudomonas fluorescens, an alpha/beta hydrolase with broad substrate specificity.
Related PDB 1auo 1aur
Related UniProtKB Q53547
[9]
Resource
Comments
Medline ID
PubMed ID
Journal Electron. J. Biotechnol
Year 1998
Volume 1
Pages 160-173
Authors Cristina M. L. Carvalho, Maria Raquel Aires-Barros, Joaquim M. S. Cabral
Title Cutinase structure, function and biocatalytic applications.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 9593202
Journal Proteins
Year 1998
Volume 31
Pages 320-33
Authors Jelsch C, Longhi S, Cambillau C
Title Packing forces in nine crystal forms of cutinase.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 10570246
Journal Biochim Biophys Acta
Year 1999
Volume 1441
Pages 185-96
Authors Longhi S, Cambillau C
Title Structure-activity of cutinase, a small lipolytic enzyme.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 10388742
Journal Biophys J
Year 1999
Volume 77
Pages 85-98
Authors Lau EY, Bruice TC
Title Consequences of breaking the Asp-His hydrogen bond of the catalytic triad: effects on the structure and dynamics of the serine esterase cutinase.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 11099798
Journal Biochimie
Year 2000
Volume 82
Pages 1015-21
Authors Egmond MR, de Vlieg J
Title Fusarium solani pisi cutinase.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 11243887
Journal J Struct Biol
Year 2000
Volume 132
Pages 180-90
Authors Hakulinen N, Tenkanen M, Rouvinen J
Title Three-dimensional structure of the catalytic core of acetylxylan esterase from Trichoderma reesei: insights into the deacetylation mechanism.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 11080636
Journal Structure
Year 2000
Volume 8
Pages 1137-46
Authors Devedjiev Y, Dauter Z, Kuznetsov SR, Jones TL, Derewenda ZS
Title Crystal structure of the human acyl protein thioesterase I from a single X-ray data set to 1.5 A.
Related PDB 1fj2
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 15923226
Journal Biophys J
Year 2005
Volume 89
Pages 999-1008
Authors Micaelo NM, Teixeira VH, Baptista AM, Soares CM
Title Water dependent properties of cutinase in nonaqueous solvents: a computational study of enantioselectivity.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 19219875
Journal Chemistry
Year 2009
Volume 15
Pages 4270-80
Authors Rutten L, Wieczorek B, Mannie JP, Kruithof CA, Dijkstra HP, Egmond MR, Lutz M, Klein Gebbink RJ, Gros P, van Koten G
Title Solid-state structural characterization of cutinase-ECE-pincer-metal hybrids.
Related PDB 3ef3 3esa 3esb 3esc 3esd
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 19810726
Journal J Am Chem Soc
Year 2009
Volume 131
Pages 15711-6
Authors Liu Z, Gosser Y, Baker PJ, Ravee Y, Lu Z, Alemu G, Li H, Butterfoss GL, Kong XP, Gross R, Montclare JK
Title Structural and functional studies of Aspergillus oryzae cutinase: enhanced thermostability and hydrolytic activity of synthetic ester and polyester degradation.
Related PDB 3gbs
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 18983850
Journal J Mol Biol
Year 2009
Volume 385
Pages 226-35
Authors Nyon MP, Rice DW, Berrisford JM, Hounslow AM, Moir AJ, Huang H, Nathan S, Mahadi NM, Bakar FD, Craven CJ
Title Catalysis by Glomerella cingulata cutinase requires conformational cycling between the active and inactive states of its catalytic triad.
Related PDB 3dcn 3dd5 3dea
Related UniProtKB

Comments
This enzyme belongs to the lipase family (subfamily of the serine hydrolase superfamily).
Cutin is a carbohydraate polymer, whose structure is very complicated and bifurcated. It is composed of C16-monomer (Palmitic acid) or C18-monomer (oleic acid) and their derivatives. An example of the structure is indicated in the compound data, L00043 in this database, accodring to the literature [1].
This enzyme has got a catalytic triad composed of serine/histidine/aspartate, and an oxyanion hole. The oxyanion hole seems to be made up by the mainchain amide groups of Ser42 and Gln121, as well as by sidechain of Ser42 (of 1agy). Thus, this enzyme catalyzes trypsin-like reaction mechanism for carboxylic ester substrates.

Created Updated
2010-01-25 2012-02-16