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Literature summary for 6.3.2.10 extracted from

  • An, Y.J.; Jeong, C.S.; Yu, J.H.; Chung, K.M.; Cha, S.S.
    Purification, crystallization and preliminary X-ray crystallographic analysis of the UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase (MurF) from Acinetobacter baumannii (2014), Acta Crystallogr. Sect. F, 70, 976-978 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene murF, recombinant expression of His-tagged selenomethionine-substituted enzyme in Escherichia coli strain B834(DE3) Acinetobacter baumannii

Crystallization (Commentary)

Crystallization (Comment) Organism
purified MurF in complex with ATP, microbatch crystallization method, mixing of 0.002 ml of 15 mg/ml protein in 150 mM NaCl, 20 mM HEPES, pH 7.4, and 1 mM DTT, with 0.002 ml of reservoir solution containing 0.1 M sodium citrate–citric acid pH 5.5, 20% PEG 3000, 22°C, X-ray diffraction structure determination and analysis at 1.90 A resolution Acinetobacter baumannii

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Acinetobacter baumannii 5829
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Acinetobacter baumannii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysine + D-alanyl-D-alanine Acinetobacter baumannii
-
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
-
?
ATP + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysine + D-alanyl-D-alanine Acinetobacter baumannii AB307-0294
-
ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
-
?

Organism

Organism UniProt Comment Textmining
Acinetobacter baumannii A0A0J9X1Z8
-
-
Acinetobacter baumannii AB307-0294 A0A0J9X1Z8
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain B834(DE3) by nickel affinity chromatography, gel filtration, and ultrafiltration Acinetobacter baumannii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysine + D-alanyl-D-alanine
-
Acinetobacter baumannii ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
-
?
ATP + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysine + D-alanyl-D-alanine
-
Acinetobacter baumannii AB307-0294 ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
-
?

Subunits

Subunits Comment Organism
? x * 50000, about, recombinant His-tagged enzyme, SDS-PAGE Acinetobacter baumannii

Synonyms

Synonyms Comment Organism
AbMurF
-
Acinetobacter baumannii
ATP-dependent UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
-
Acinetobacter baumannii
MurF
-
Acinetobacter baumannii

Cofactor

Cofactor Comment Organism Structure
ATP
-
Acinetobacter baumannii

General Information

General Information Comment Organism
metabolism MurF is the enzyme responsible for the last step in the biosynthesis of UDP-N-acetylmuramyl-pentapeptide, the monomeric precursor of peptidoglycan Acinetobacter baumannii
physiological function MurF is the enzyme responsible for the last step in the biosynthesis of UDP-N-acetylmuramyl-pentapeptide, the monomeric precursor of peptidoglycan. MurF catalyzes the addition of D-Ala-D-Ala dipeptide to UDP-N-acetylmuramyl-tripeptide [UDPMurNAc-L-Ala-gamma-D-Glu-m-DAP(or L-Lys)] in an ATP-dependent manner. The gamma-phosphate of ATP is transferred to the C-terminal carboxylate of UDP-N-acetylmuramyl-tripeptide to form an acyl phosphate intermediate, which is subsequently attacked by the amino group of the incoming dipeptide to form a peptide bond in a non-ribosomal fashion Acinetobacter baumannii