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Overview for MACiE Entry M0291

Version history

General Information

EC Number: 2.3.1.39 (A member of the Transferases, Acyltransferases, Transferring groups other than aminoacyl groups)

Enzyme Name: malonyl-CoA-acyl carrier protein transacylase

Biological Species: Escherichia coli (Bacteria)

Catalytic Chain UniprotKB Accession Codes:

  • P0AAI9 - Malonyl CoA-acyl carrier protein transacylase

Representative PDB Code: 1mla - THE ESCHERICHIA COLI MALONYL-COA:ACYL CARRIER PROTEINTRANSACYLASE AT 1.5-ANGSTROMS RESOLUTION. CRYSTALSTRUCTURE OF A FATTY ACID SYNTHASE COMPONENT (Resolution = 1.50 Å).

Catalytic CATH Codes:

  • 3.40.366.10 - Malonyl-Coenzyme A Acyl Carrier Protein, domain 2

"Other" CATH Codes:

Display structure information

Overall Reaction:

Image of acyl-carrier protein

Image of malonyl-CoA

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Image of CoA

Image of malonyl-[acyl-carrier protein]

acyl-carrier protein
C00229
CHEBI:13534
malonyl-CoA
C00083
CHEBI:15531
CoA
C00010
CHEBI:57287
malonyl-[acyl-carrier protein]
C01209
CHEBI:17330

Overall Comment: Malonyl-CoA-acyl carrier protein transacylase, along with Acyl-carrier-protein S-acetyltransferase (EC 2.3.1.38), is essential for the initiation of fatty-acid biosynthesis in bacteria. This enzyme also provides the malonyl groups for polyketide biosynthesis [4].


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Stepwise Description of the Reaction

Step 1Ser92 is activated towards nucleophilic attack at the thio-carbonyl of malonyl-CoA by the general base His201.
Step 2The tetrahedral enzyme-substrate intermediate collapses, eliminating the coenzyme A component.
Step 3The terminal thiolate of the previously eliminated CoA acts as a general base towards His201.
Step 4The enzyme-malonyl carbonyl linkage acts as an electrophile towards the terminal thiol of the acyl carrier protein which is deprotonated by the general acid His201.
Step 5The tetrahedral intermediate collapses eliminating the malonyl acyl-carrier protein adduct and free serine side chain, which is reprotonated by the general acid His201A.

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Catalytic Residues Involved

Type Number Chain Location of Function
Ser 92 A Side Chain
Leu 93 A Main Chain Amide
His 201 A Side Chain
Arg 117 A Side Chain
Gln 250 A Main Chain Carbonyl
Gln 11 A Side Chain

References

  1. L. Serre et al. (1995), J. Biol. Chem., 270, 12961-12964. The Escherichia coli malonyl-CoA:acyl carrier protein transacylase at 1.5-A resolution. Crystal structure of a fatty acid synthase component.
    Medline: 7768883
  2. V. C. Joshi (1972), Biochem. J., 128, 43-44. Mechanism of malonyl-coenzyme A-acyl-carrier protein transacylase.
    Medline: 4563767
  3. L. Serre et al. (1994), J. Mol. Biol., 242, 99-102. Crystallization of the malonyl coenzyme A-acyl carrier protein transacylase from Escherichia coli.
    Medline: 8078074

Homologue information for M0291 (1mla)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)


Links to this entry in other databases

Link to EC-PDB-SUM Link to PDB-SUM Link to RCSB PDB Link to PDBe Link to CSA
Link to MetaCyc Link to KEGG Link to BRENDA Link to ExplorENZ
Link to EzCatDB

GOA logo
catalytic activity (molecular function)
[acyl-carrier-protein] S-malonyltransferase activity (molecular function)
binding (molecular function)
fatty acid biosynthetic process (biological process)
metabolic process (biological process)
transferase activity (molecular function)
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