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, |
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, |
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, |
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, |
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, This enzyme has got a catalytic triad composed of serine/histidine/aspartate, |
Created | Updated |
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2010-01-25 | 2012-02-16 |