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Literature summary 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)

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 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

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 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
-
 Acinetobacter baumannii AB307-0294 ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
-
 ?

Subunits

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

Synonyms

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

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.2.10 ATP
-
 Acinetobacter baumannii

General Information

EC Number General Information Comment Organism
6.3.2.10 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
6.3.2.10 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