_EC 2.3.1.7 Carnitine O-acetyltransferase. 11 PDB entries  
EC 2.-.-.- Transferases. [17,943 PDB entries]
EC 2.3.-.- Acyltransferases. [1,208 PDB entries]
EC 2.3.1.- Transferring groups other than amino-acyl groups. [998 PDB entries]
EC 2.3.1.7 Carnitine O-acetyltransferase. [11 PDB entries]    
1ndb

Reaction: Acetyl-CoA + carnitine = CoA + O-acetylcarnitine.
 


Acetyl-CoA
+
carnitine
=
CoA
+
O-acetylcarnitine
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Other name(s): Carnitine acetylase.
Comments: Also acts on propanoyl-CoA and butanoyl-CoA (cf. Ec 2.3.1.21 and Ec 2.3.1.137).
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 11 PDB entries in enzyme class E.C.2.3.1.7

  PDB code Protein
1ndb
Crystal structure of carnitine acetyltransferase
Source: Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (596 residues) CATH domains: Unassigned Unassigned
1ndf
Carnitine acetyltransferase in complex with carnitine
Source: Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (596 residues) CATH domains: Unassigned Unassigned
Bound ligand:   Het Group 152 corresponds to enzyme reactant Carnitine
1ndi
Carnitine acetyltransferase in complex with coa
Source: Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (596 residues) CATH domains: Unassigned Unassigned
Bound ligand:   Het Group COA is 94.00% similar to enzyme reactant acetyl-CoA
1nm8
Structure of human carnitine acetyltransferase: molecular basis for fatty acyl transfer
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: crat or cat1. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (591 residues) CATH domains: Unassigned Unassigned
1s5o
Structural and mutational characterization of l-carnitine binding to human carnitine acetyltransferase
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (591 residues) CATH domains: Unassigned Unassigned
Bound ligand:   Het Group 152 corresponds to enzyme reactant Carnitine
1t7n
Crystal structure of the m564g mutant of murine crat
Source: Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (599 residues) CATH domains: Unassigned Unassigned
1t7o
Crystal structure of the m564g mutant of murine carnitine acetyltransferase in complex with carnitine
Source: Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (599 residues) CATH domains: Unassigned Unassigned
Bound ligand:   Het Group 152 corresponds to enzyme reactant Carnitine
1t7q
Crystal structure of the f565a mutant of murine carnitine acetyltransferase in complex with carnitine and coa
Source: Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (599 residues) CATH domains: Unassigned Unassigned
Bound ligands:   Het Group COA is 94.00% similar to enzyme reactant acetyl-CoA
  Het Group 152 corresponds to enzyme reactant Carnitine
2h3p
Crystal structure of murine carnitine acetyltransferase in complex with carnitine and acetyl-coa
Source: Mus musculus. House mouse. Organism_taxid: 10090. Gene: crat. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (599 residues) CATH domains: Unassigned Unassigned
Bound ligands:   Het Group ACO corresponds to enzyme reactant acetyl-CoA
  Het Group 152 corresponds to enzyme reactant Carnitine
2h3u
Crystal structure of murine carnitine acetyltransferase in complex with carnitine and coa
Source: Mus musculus. House mouse. Organism_taxid: 10090. Gene: crat. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (599 residues) CATH domains: Unassigned Unassigned
Bound ligands:   Het Group COA is 94.00% similar to enzyme reactant acetyl-CoA
  Het Group 152 corresponds to enzyme reactant Carnitine
2h3w
Crystal structure of the s554a/m564g mutant of murine carnitine acetyltransferase in complex with hexanoylcarnitine and coa
Source: Mus musculus. House mouse. Organism_taxid: 10090. Gene: crat. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (599 residues) CATH domains: Unassigned Unassigned
Bound ligands:   Het Group COA is 94.00% similar to enzyme reactant acetyl-CoA
  Het Group HC5 is 77.00% similar to enzyme product O-acetylcarnitine