_EC 3.1.2.14 Oleoyl-[acyl-carrier-protein] hydrolase. 17 PDB entries  
EC 3.-.-.- Hydrolases. [22,185 PDB entries]
EC 3.1.-.- Acting on ester bonds. [6,208 PDB entries]
EC 3.1.2.- Thiolester hydrolases. [90 PDB entries]
EC 3.1.2.14 Oleoyl-[acyl-carrier-protein] hydrolase. [17 PDB entries]    
1xkt

Reaction: Oleoyl-[acyl-carrier-protein] + H(2)O = [acyl-carrier-protein] + oleate.
 


Oleoyl-[acyl-carrier-protein]
+ H(2)O
=
[acyl-carrier-protein]
+
oleate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Other name(s): Acyl-[acyl-carrier-protein] hydrolase. S-acyl fatty acid synthase thioesterase.
Comments: Acts on [acyl-carrier-protein] thioesters of fatty acids from C(12) to C(18), but the derivative of oleic acid is hydrolyzed much more rapidly than any other compound tested.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 17 PDB entries in enzyme class E.C.3.1.2.14

  PDB code Protein
1xkt
Human fatty acid synthase: structure and substrate selectivity of the thioesterase domain
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (260 residues) CATH domains: 3.40.50.1820 1.10.1470.20
1xxy
Theoretical model of the arabidopsis thaliana fatb acyl-acp thioesterase
Source: Arabidopsis thaliana. Thale cress. Thale cress
Chains: X, Y (131 residues)
2cg5
Structure of aminoadipate-semialdehyde dehydrogenase- phosphopantetheinyl transferase in complex with cytosolic acyl carrier protein and coenzyme a
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693. Expression_system_cell_line: de3. Expressed in: escherichia coli
Chain: B (71 residues) CATH domain: 1.10.1200.10
2jfd
Structure of the mat domain of human fas
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693. Expression_system_cell_line: de3-r3.
Chains: A, B, C, D (404 residues) CATH domains: Unassigned 3.40.366.10 3.30.70.250
2jfk
Structure of the mat domain of human fas with malonyl-coa
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693. Expression_system_cell_line: de3-r3.
Chains: A, B, C, D (401 residues) CATH domains: Unassigned 3.40.366.10 3.30.70.250
2own
Crystal structure of oleoyl thioesterase (putative) (np_7844 lactobacillus plantarum at 2.00 a resolution
Source: Lactobacillus plantarum. Organism_taxid: 1590. Strain: ncimb 8826, wcfs1. Atcc: baa-793. Gene: np_784467.1, fat, lp_0708. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (256 residues)
2pff
Structural insights of yeast fatty acid synthase
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Strain: yit613. Synthetic: yes
Chains: B, E, H (2006 residues) CATH domains: Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned
2png
Type i rat fatty acid synthase acyl carrier protein (acp) domain
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Gene: fasn. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chain: A (89 residues) CATH domain: 1.10.1200.10
2px6
Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by orlistat
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: fas. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (253 residues) CATH domains: 3.40.50.1820 1.10.1470.20
Bound ligand:   Het Group DH9 is 48.00% similar to enzyme product oleate
2uv8
Crystal structure of yeast fatty acid synthase with stalled acyl carrier protein at 3.1 angstrom resolution
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Organism_taxid: 4932
Chains: G, H, I (2033 residues) CATH domains: Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned
2vkz
Structure of the cerulenin-inhibited fungal fatty acid synthase type i multienzyme complex
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Organism_taxid: 4932
Chains: G, H, I (2033 residues) CATH domains: Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned
3hhd
Structure of the human fatty acid synthase ks-mat didomain as a framework for inhibitor design.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: fasn, fas. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108
Chains: A, B, C, D (852 residues) CATH domains: Unassigned Unassigned Unassigned 3.30.70.250
3hmj
Saccharomyces cerevisiae fas type i
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: fas2. Gene: fas1
Chains: G, H, I (2033 residues) CATH domains: Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned
3tjm
Crystal structure of the human fatty acid synthase thioester with an activate site-specific polyunsaturated fatty acyl a
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: fas, fasn. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chain: A (275 residues) CATH domains: 3.40.50.1820 1.10.1470.20
4piv
Human fatty acid synthase psi/kr tri-domain with NADPH and g
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: fasn, fas. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108.
Chains: A, B (610 residues) CATH domains: Unassigned Unassigned
4w82
Enoyl-acyl carrier protein-reductase domain from human fatty synthase
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: fasn, fas. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_cell_line: 2566.
Chains: A, B (306 residues) CATH domains: Unassigned 3.40.50.720
4w9n
Enoyl-acyl carrier protein-reductase domain from human fatty synthase complexed with triclosan
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: fasn, fas. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (323 residues) CATH domains: Unassigned 3.40.50.720