| Accepted Name |
|---|
| [acyl-carrier-protein] S-malonyltransferase.
|
| Alternative Name(s) |
|---|
| acyl carrier protein malonyltransferase. |
| malonyl-CoA/dephospho-CoA acyltransferase. |
| malonyl-CoA-acyl carrier protein transacylase. |
| malonyl coenzyme A-acyl carrier protein transacylase. |
| malonyl transacylase. |
| malonyl transferase. |
| MCAT. |
| Reaction catalysed |
|---|
| holo-[ACP] + malonyl-CoA <=> CoA + malonyl-[ACP] |
| Comment(s) |
|---|
- Essential, along with EC 2.3.1.38, for the initiation of fatty-acid
biosynthesis in bacteria.
- Also provides the malonyl groups for polyketide biosynthesis.
- The product of the reaction, malonyl-ACP, is an elongation substrate
in fatty-acid biosynthesis.
- In Mycobacterium tuberculosis, holo-ACP (the product of EC 2.7.8.7)
is the preferred substrate.
- This enzyme also forms part of the multienzyme complexes EC 4.1.1.88
and EC 4.1.1.89.
- Malonylation of ACP is immediately followed by decarboxylation within
the malonate-decarboxylase complex to yield acetyl-ACP,
the catalytically active species of the decarboxylase.
- In the enzyme from Klebsiella pneumoniae, methylmalonyl-CoA can also
act as a substrate but acetyl-CoA cannot whereas the enzyme from
Pseudomonas putida can use both as substrates.
- The ACP subunit found in fatty-acid biosynthesis contains a
pantetheine-4'-phosphate prosthetic group; that from malonate
decarboxylase also contains pantetheine-4'-phosphate but in the form
of a 2'-(5-triphosphoribosyl)-3'-dephospho-CoA prosthetic group.
|
| Cross-references |
|---|
| BRENDA | 2.3.1.39 |
| EC2PDB | 2.3.1.39 |
| ExplorEnz | 2.3.1.39 |
| PRIAM enzyme-specific profiles | 2.3.1.39 |
| KEGG Ligand Database for Enzyme Nomenclature | 2.3.1.39 |
| IUBMB Enzyme Nomenclature | 2.3.1.39 |
| IntEnz | 2.3.1.39 |
| MEDLINE | Find literature relating to 2.3.1.39 |
| MetaCyc | 2.3.1.39 |
| Rhea expert-curated reactions | 2.3.1.39 |
| UniProtKB/Swiss-Prot |
| Q8TGA1, AFLB_ASPPU; | Q5AV07, ATNM_EMENI; | A7Z4X8, BAEC_BACVZ; |
| A7Z4Y0, BAEE_BACVZ; | P71019, FABD_BACSU; | Q8K9J6, FABD_BUCAP; |
| Q89AH0, FABD_BUCBP; | Q8T3L6, FABD_DROME; | Q8X8I7, FABD_ECO57; |
| P0AAJ0, FABD_ECOL6; | P0AAI9, FABD_ECOLI; | P43712, FABD_HAEIN; |
| Q8IVS2, FABD_HUMAN; | Q8R3F5, FABD_MOUSE; | P63459, FABD_MYCBO; |
| A0R0B2, FABD_MYCS2; | P9WNG4, FABD_MYCTO; | P9WNG5, FABD_MYCTU; |
| O85140, FABD_SALTY; | O13698, FABD_SCHPO; | Q5HGK3, FABD_STAAC; |
| Q99UN8, FABD_STAAM; | Q7A5Z3, FABD_STAAN; | Q6GHK5, FABD_STAAR; |
| Q6G9Y3, FABD_STAAS; | Q93QD4, FABD_STAAU; | Q7A124, FABD_STAAW; |
| P73242, FABD_SYNY3; | Q12283, FABD_YEAST; | P34731, FAS1_CANAX; |
| Q9UUG0, FAS1_SCHPO; | P34229, FAS1_YARLI; | P07149, FAS1_YEAST; |
| Q71SP7, FAS_BOVIN; | P12276, FAS_CHICK; | P49327, FAS_HUMAN; |
| P19096, FAS_MOUSE; | P12785, FAS_RAT; | Q9R9J2, FENF_BACIU; |
| I1S489, GRA7_GIBZE; | M2XHU6, HEXB_DOTSN; | Q2TXG3, ORYB_ASPOR; |
| A0A1U8QK63, PKIC_EMENI; | O34825, PKSC_BACSU; | O34787, PKSE_BACSU; |
| Q00706, STCK_EMENI; | Q2T4N0, THAF_BURTA; | Q92215, TOXC_COCCA; |
|