EzCatDB: S00724
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DB codeS00724
RLCP classification1.12.30000.27 : Hydrolysis
CATH domainDomain 13.40.50.1820 : Rossmann foldCatalytic domain
E.C.3.1.1.74
CSA1agy

CATH domainRelated DB codes (homologues)
3.40.50.1820 : Rossmann foldS00544,S00344,S00517,S00525,S00526,S00720,S00723,S00725,S00919,S00057,S00374,S00345,S00347,S00348,S00346,S00350,S00352,S00353,S00355,S00356,S00358,D00189,D00210,D00539,T00253

Enzyme Name
UniProtKBKEGG

P00590P11373P52956
Protein nameCutinase 1Cutinase 1Cutinase 1Cutinase
SynonymsEC 3.1.1.74
Cutin hydrolase 1
EC 3.1.1.74
Cutin hydrolase 1
EC 3.1.1.74
Cutin hydrolase 1
L1
RefSeq

XP_001817153.1 (Protein)
XM_001817101.2 (DNA/RNA sequence)
PfamPF01083 (Cutinase)
[Graphical view]
PF01083 (Cutinase)
[Graphical view]
PF01083 (Cutinase)
[Graphical view]


UniProtKB:Accession NumberP00590P11373P52956
Entry nameCUTI1_FUSSOCUTI1_COLGLCUTI1_ASPOR
ActivityCutin + H2O = cutin monomers.Cutin + H2O = cutin monomers.Cutin + H2O = cutin monomers.
Subunit


Subcellular locationSecreted.Secreted.Secreted.
Cofactor



Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idL00043C00001L00068L00067L00044L00069L00070L00071L00072I00123I00085I00086
CompoundCutinH2OC16 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
Typecarbohydrate,fatty acidH2Ocarbohydrate,fatty acidcarbohydrate,fatty acidcarbohydrate,fatty acidcarbohydrate,fatty acidcarbohydrate,fatty acidcarbohydrate,fatty acidcarbohydrate,fatty acid


ChEBI
15377
15756
55328

16196
79312





PubChem
962
22247451
985
10466
322588
445639
5312773
9818312
5282938



                    
1agyA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cexA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cuaA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cubA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cucA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cudA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cudB00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cudC00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cueA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cufA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cugA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cuhA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cuiA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cujA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cusA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cuuA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cuvA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cuwA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cuwB00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cuxA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cuyA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1cuzA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ffaA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ffbA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ffcA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ffdA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ffeA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1oxmA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:TC4UnboundUnbound
1oxmB00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:TC4UnboundUnbound
1xzaA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1xzbA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1xzcA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1xzdA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1xzeA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1xzfA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1xzgA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1xzhA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1xziA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1xzjA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1xzkA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:DFPUnboundUnbound
1xzkB00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:DFPUnboundUnbound
1xzlA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:HEEUnboundUnbound
1xzmA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:DPEUnboundUnbound
2cutA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:DEPUnboundUnbound
3ef3A00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:NXCUnboundUnbound
3esaA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:NXCUnboundUnbound
3esaB00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:NXCUnboundUnbound
3esbA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:NXCUnboundUnbound
3escA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:SXCUnboundUnbound
3esdA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:SXCUnboundUnbound
3dcnA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3dd5A00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:DEPUnboundUnbound
3dd5B00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:DEPUnboundUnbound
3dd5C00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:DEPUnboundUnbound
3dd5D00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:DEPUnboundUnbound
3dd5E00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:DEPUnboundUnbound
3dd5F00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:DEPUnboundUnbound
3dd5G00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:DEPUnboundUnbound
3dd5H00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:DEPUnboundUnbound
3deaA00Analogue:HZH UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3deaB00Analogue:HZH UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
3gbsA00Unbound UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
literature [2], [3], [4], [11], [12], [13], [16], [19]
pdbCatalytic residuesMain-chain involved in catalysiscomment
           
1agyA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
 
1cexA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A
1cuaA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, N172K
1cubA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, N172K, R196D
1cucA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, N172K, R196D
1cudA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, N172K, R196D
1cudB00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, N172K, R196D
1cudC00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, N172K, R196D
1cueA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, Q121L
1cufA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, R156I
1cugA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, R17E, N172K
1cuhA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, R196E
1cuiA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, S120A
1cujA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, S120C
1cusA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A
1cuuA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, A199C
1cuvA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, A85F
1cuwA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, G82A, A85F, V184I, A185L, L189F
1cuwB00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, G82A, A85F, V184I, A185L, L189F
1cuxA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, I114Y
1cuyA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, I189F
1cuzA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, I81G, I182G
1ffaA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant N84A
1ffbA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant N84D
1ffcA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant N84L
1ffdA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant N84W
1ffeA00      ;SER 120;ASP 175;HIS 188
      ;GLN 121
mutant S42A
1oxmA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A
1oxmB00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A
1xzaA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, S129C
1xzbA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, S129C
1xzcA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, S129C
1xzdA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, S213C
1xzeA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, S92C
1xzfA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, T144C
1xzgA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, T45A
1xzhA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, T80P
1xziA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, Y119H
1xzjA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, Y38F
1xzkA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A
1xzkB00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A
1xzlA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A
1xzmA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A
2cutA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A
3ef3A00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, N172K
3esaA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, N172K
3esaB00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, N172K
3esbA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, N172K
3escA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, N172K
3esdA00SER 42;SER 120;ASP 175;HIS 188
SER 42;GLN 121
mutant R32A, N172K
3dcnA00SER 57;SER 136;ASP 191;HIS 204
SER 57;GLN 137
 
3dd5A00SER 57;SER 136;ASP 191;HIS 204
SER 57;GLN 137
 
3dd5B00SER 57;SER 136;ASP 191;HIS 204
SER 57;GLN 137
 
3dd5C00SER 57;SER 136;ASP 191;HIS 204
SER 57;GLN 137
 
3dd5D00SER 57;SER 136;ASP 191;HIS 204
SER 57;GLN 137
 
3dd5E00SER 57;SER 136;ASP 191;HIS 204
SER 57;GLN 137
 
3dd5F00SER 57;SER 136;ASP 191;HIS 204
SER 57;GLN 137
 
3dd5G00SER 57;SER 136;ASP 191;HIS 204
SER 57;GLN 137
 
3dd5H00SER 57;SER 136;ASP 191;HIS 204
SER 57;GLN 137
 
3deaA00SER 57;SER 136;ASP 191;       
SER 57;GLN 137
invisible 197-204
3deaB00SER 57;SER 136;ASP 191;       
SER 57;GLN 137
invisible 201-204
3gbsA00SER 48;SER 126;ASP 181;HIS 194
SER 48;GLN 127
 

References for Catalytic Mechanism
ReferencesSectionsNo. 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]
PubMed ID17779010
JournalScience
Year1980
Volume208
Pages990-1000
AuthorsKolattukudy PE
TitleBiopolyester membranes of plants: cutin and suberin.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
PubMed ID1560844
JournalNature
Year1992
Volume356
Pages615-8
AuthorsMartinez C, De Geus P, Lauwereys M, Matthyssens G, Cambillau C
TitleFusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent.
Related PDB1cus
Related UniProtKBP00590
[3]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
PubMed ID8286366
JournalBiochemistry
Year1994
Volume33
Pages83-9
AuthorsMartinez C, Nicolas A, van Tilbeurgh H, Egloff MP, Cudrey C, Verger R, Cambillau C
TitleCutinase, a lipolytic enzyme with a preformed oxyanion hole.
Related PDB2cut
Related UniProtKBP00590
[4]
PubMed ID8555209
JournalBiochemistry
Year1996
Volume35
Pages398-410
AuthorsNicolas A, Egmond M, Verrips CT, de Vlieg J, Longhi S, Cambillau C, Martinez C
TitleContribution of cutinase serine 42 side chain to the stabilization of the oxyanion transition state.
Related PDB1ffa,1ffb,1ffc,1ffd,1ffe
[5]
PubMed ID8990497
JournalProteins
Year1996
Volume26
Pages442-58
AuthorsLonghi S, Nicolas A, Creveld L, Egmond M, Verrips CT, de Vlieg J, Martinez C, Cambillau C
TitleDynamics of Fusarium solani cutinase investigated through structural comparison among different crystal forms of its variants.
Related PDB1cua,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
[6]
CommentsX-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 17-230.
PubMed ID9175860
JournalJ Mol Biol
Year1997
Volume268
Pages779-99
AuthorsLonghi S, Czjzek M, Lamzin V, Nicolas A, Cambillau C
TitleAtomic resolution (1.0 A) crystal structure of Fusarium solani cutinase: stereochemical analysis.
Related PDB1agy,1cex
Related UniProtKBP00590
[7]
PubMed ID9041628
JournalProtein Sci
Year1997
Volume6
Pages275-86
AuthorsLonghi S, Mannesse M, Verheij HM, De Haas GH, Egmond M, Knoops-Mouthuy E, Cambillau C
TitleCrystal structure of cutinase covalently inhibited by a triglyceride analogue.
Related PDB1oxm
[8]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed ID9438866
JournalStructure
Year1997
Volume5
Pages1571-84
AuthorsKim KK, Song HK, Shin DH, Hwang KY, Choe S, Yoo OJ, Suh SW
TitleCrystal structure of carboxylesterase from Pseudomonas fluorescens, an alpha/beta hydrolase with broad substrate specificity.
Related PDB1auo,1aur
Related UniProtKBQ53547
[9]
JournalElectron. J. Biotechnol
Year1998
Volume1
Pages160-173
AuthorsCristina M. L. Carvalho, Maria Raquel Aires-Barros, Joaquim M. S. Cabral
TitleCutinase structure, function and biocatalytic applications.
[10]
PubMed ID9593202
JournalProteins
Year1998
Volume31
Pages320-33
AuthorsJelsch C, Longhi S, Cambillau C
TitlePacking forces in nine crystal forms of cutinase.
[11]
PubMed ID10570246
JournalBiochim Biophys Acta
Year1999
Volume1441
Pages185-96
AuthorsLonghi S, Cambillau C
TitleStructure-activity of cutinase, a small lipolytic enzyme.
[12]
PubMed ID10388742
JournalBiophys J
Year1999
Volume77
Pages85-98
AuthorsLau EY, Bruice TC
TitleConsequences of breaking the Asp-His hydrogen bond of the catalytic triad: effects on the structure and dynamics of the serine esterase cutinase.
[13]
PubMed ID11099798
JournalBiochimie
Year2000
Volume82
Pages1015-21
AuthorsEgmond MR, de Vlieg J
TitleFusarium solani pisi cutinase.
[14]
PubMed ID11243887
JournalJ Struct Biol
Year2000
Volume132
Pages180-90
AuthorsHakulinen N, Tenkanen M, Rouvinen J
TitleThree-dimensional structure of the catalytic core of acetylxylan esterase from Trichoderma reesei: insights into the deacetylation mechanism.
[15]
PubMed ID11080636
JournalStructure
Year2000
Volume8
Pages1137-46
AuthorsDevedjiev Y, Dauter Z, Kuznetsov SR, Jones TL, Derewenda ZS
TitleCrystal structure of the human acyl protein thioesterase I from a single X-ray data set to 1.5 A.
Related PDB1fj2
[16]
PubMed ID15923226
JournalBiophys J
Year2005
Volume89
Pages999-1008
AuthorsMicaelo NM, Teixeira VH, Baptista AM, Soares CM
TitleWater dependent properties of cutinase in nonaqueous solvents: a computational study of enantioselectivity.
[17]
PubMed ID19219875
JournalChemistry
Year2009
Volume15
Pages4270-80
AuthorsRutten L, Wieczorek B, Mannie JP, Kruithof CA, Dijkstra HP, Egmond MR, Lutz M, Klein Gebbink RJ, Gros P, van Koten G
TitleSolid-state structural characterization of cutinase-ECE-pincer-metal hybrids.
Related PDB3ef3,3esa,3esb,3esc,3esd
[18]
PubMed ID19810726
JournalJ Am Chem Soc
Year2009
Volume131
Pages15711-6
AuthorsLiu Z, Gosser Y, Baker PJ, Ravee Y, Lu Z, Alemu G, Li H, Butterfoss GL, Kong XP, Gross R, Montclare JK
TitleStructural and functional studies of Aspergillus oryzae cutinase: enhanced thermostability and hydrolytic activity of synthetic ester and polyester degradation.
Related PDB3gbs
[19]
PubMed ID18983850
JournalJ Mol Biol
Year2009
Volume385
Pages226-35
AuthorsNyon MP, Rice DW, Berrisford JM, Hounslow AM, Moir AJ, Huang H, Nathan S, Mahadi NM, Bakar FD, Craven CJ
TitleCatalysis by Glomerella cingulata cutinase requires conformational cycling between the active and inactive states of its catalytic triad.
Related PDB3dcn,3dd5,3dea

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.

createdupdated
2010-01-252012-02-16


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 2008)
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)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
© Biotechnology Research Institute for Drug Discovery, AIST, 2015-2016 All Rights Reserved.
© Computational Biology Research Center, AIST, 2004-2016 All Rights Reserved.