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Literature summary extracted from

  • Cha, S.S.; An, Y.J.; Jeong, C.S.; Yu, J.H.; Chung, K.M.
    ATP-binding mode including a carbamoylated lysine and two Mg(2+) ions, and substrate-binding mode in Acinetobacter baumannii MurF (2014), Biochem. Biophys. Res. Commun., 450, 1045-1050 .
    View publication on PubMed

Application

EC Number Application Comment Organism
6.3.2.10 drug development AbMurF is a target for the structure-based development of inhibitors to treat Acinetobacter baumannii infections Acinetobacter baumannii

Cloned(Commentary)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.3.2.10 crystallization of two MurF-ATP complexes: the MurF–ATP complex and the MurF-ATP-UDP complex, trigonal crystals of Se-AbMurF with ATP are grown in a precipitant solution containing 20% w/v PEG 3000 and 0.1 M sodium citrate-citric acid, pH 5.5, crystals of the AbMurF-ATP-UDP complex are obtained by soaking experiments, trigonal crystals of the AbMurF-ATP complex isomorphous to those of the Se-AbMurF-ATP complex are grown in the mother liquor and are then transferred to a solution containing 20% glycerol, 20% PEG 3000, 0.1 M sodium citrate-citric acid, pH 5.5, and 15 mM UDP, 25 min soaking, monoclinic crystals of the AbMurF-ATP complex are grown in a precipitant solution containing 24% PEG 4000, 0.08 M Tris-HCl, pH 8.5, 0.16 M MgCl2, and 20% glycerol by the micro-batch crystallization method at 22°C, X-ray diffraction structure determination and analysis at 1.8-2.8 A resolution Acinetobacter baumannii

Localization

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.2.10 Mg2+ required, the ATP-binding mode revealed by the crystal structure of the MurF-ATP complex confirms that a carbamoylated lysine and two Mg2+ ions are required for enzyme activity of MurF Acinetobacter baumannii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.2.10 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
-
 ?
6.3.2.10 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

EC Number Organism UniProt Comment Textmining
6.3.2.10 Acinetobacter baumannii A0A0J9X1Z8
-
-
6.3.2.10 Acinetobacter baumannii AB307-0294 A0A0J9X1Z8
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.2.10 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
-
 ?
6.3.2.10 ATP + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysine + D-alanyl-D-alanine ATP and UDP binding mode analysis, overview Acinetobacter baumannii ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
-
 ?
6.3.2.10 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
-
 ?
6.3.2.10 ATP + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysine + D-alanyl-D-alanine ATP and UDP binding mode analysis, overview Acinetobacter baumannii AB307-0294 ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
-
 ?
6.3.2.10 additional information the ATP-binding mode revealed by the crystal structure of the MurF-ATP complex confirms that a carbamoylated lysine and two Mg2+ ions are required for enzyme activity of MurF. UDP-MurF interactions are observed in the crystal structure of the MurF-ATP-UDP complex, depicting the characteristic substrate-binding mode of MurF. Structure-function analysis, overview Acinetobacter baumannii ?
-
 ?
6.3.2.10 additional information the ATP-binding mode revealed by the crystal structure of the MurF-ATP complex confirms that a carbamoylated lysine and two Mg2+ ions are required for enzyme activity of MurF. UDP-MurF interactions are observed in the crystal structure of the MurF-ATP-UDP complex, depicting the characteristic substrate-binding mode of MurF. Structure-function analysis, overview Acinetobacter baumannii AB307-0294 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.3.2.10 AbMurF
-
 Acinetobacter baumannii
6.3.2.10 MurF
-
 Acinetobacter baumannii

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.2.10 ATP the ATP-binding mode revealed by the crystal structure of the MurF-ATP complex confirms that a carbamoylated lysine and two Mg2+ ions are required for enzyme activity of MurF Acinetobacter baumannii

General Information

EC Number General Information Comment Organism
6.3.2.10 physiological function MurF adds D-Ala-D-Ala dipeptide to UDP-N-acetylmuramyl-L-Ala-c-D-Glu-m-DAP (or L-Lys) in an ATP-dependent manner, which is the last step in the biosynthesis of monomeric precursor of peptidoglycan for bacterial cell wall synthesis Acinetobacter baumannii