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Literature summary for 1.3.1.98 extracted from

  • Naqvi, K.F.; Patin, D.; Wheatley, M.S.; Savka, M.A.; Dobson, R.C.; Gan, H.M.; Barreteau, H.; Blanot, D.; Mengin-Lecreulx, D.; Hudson, A.O.
    Identification and partial characterization of a novel UDP-N-acetylenolpyruvoylglucosamine reductase/UDP-N-acetylmuramate L-alanine ligase fusion enzyme from Verrucomicrobium spinosum DSM 4136(T) (2016), Front. Microbiol., 7, 362 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene murB, Verrucomicrobium spinosum possesses a fusion open reading frame annotated by the locus tag (VspiD_010100018130). Recombinant expression in Escherichia coli strain Rosetta (DE3) pLysS. The ORF, which is predicted to encode the enzymes UDP-N-acetylenolpyruvoylglucosamine reductase (MurB) and UDP-N-acetylmuramate:L-alanine ligase (MurC) is cloned. In vivo analyses using functional complementation shows that the fusion gene is able to functionally complement Escherichia coli murB (mutant ST5 strain) and murC temperature sensitive mutants. The purified recombinant fusion enzyme (MurB/CVs) is endowed with UDP-N-acetylmuramate:L-alanine ligase activity. All attempts to demonstrate an in vitro UDP-N-acetylenolpyruvoylglucosamine reductase (MurB) activity are unsuccessful. Phylogenetic analysis reveals that this fusion enzyme can only be identified in specific lineages within the Verrucomicrobia phylum. The fusion gene is able to functionally complement two Escherichia coli strains that harbor mutations in the murB and murC genes Verrucomicrobium spinosum

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Verrucomicrobium spinosum 5737
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine + NADPH + H+ Verrucomicrobium spinosum the enzyme MurB catalyzes the reduction of the enolpyruvyl moiety of UDP-GlcNAc-enolpyruvate to lactyl ether to produce UDP-N-acetylmuramic acid UDP-N-acetyl-alpha-D-muramate + NADP+
-
?

Organism

Organism UniProt Comment Textmining
Verrucomicrobium spinosum
-
-
-
Verrucomicrobium spinosum DSM 4136
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine + NADPH + H+
-
Verrucomicrobium spinosum UDP-N-acetyl-alpha-D-muramate + NADP+
-
?
UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine + NADPH + H+ the enzyme MurB catalyzes the reduction of the enolpyruvyl moiety of UDP-GlcNAc-enolpyruvate to lactyl ether to produce UDP-N-acetylmuramic acid Verrucomicrobium spinosum UDP-N-acetyl-alpha-D-muramate + NADP+
-
?
UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine + NADPH + H+
-
Verrucomicrobium spinosum DSM 4136 UDP-N-acetyl-alpha-D-muramate + NADP+
-
?

Subunits

Subunits Comment Organism
? x * 87300, recombinant MurB/CVs fusion enzyme, SDS-PAGE Verrucomicrobium spinosum
More domain mapping of the MurB/CVs fusion enzyme of Verrucomicrobium spinosum and the individual MurB and MurC enzymes from Escherichia coli Verrucomicrobium spinosum

Synonyms

Synonyms Comment Organism
MurB
-
Verrucomicrobium spinosum
MurBAb
-
Verrucomicrobium spinosum
UDP-N-acetylenolpyruvoylglucosamine reductase
-
Verrucomicrobium spinosum
VspiD_010100018130 locus name Verrucomicrobium spinosum

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Verrucomicrobium spinosum

General Information

General Information Comment Organism
evolution Verrucomicrobium spinosum possesses a fusion open reading frame annotated by the locus tag (VspiD_010100018130). The ORF, which is predicted to encode the enzymes UDP-N-acetylenolpyruvoylglucosamine reductase (MurB) and UDP-N-acetylmuramate:L-alanine ligase (MurC) is cloned. In vivo analyses using functional complementation shows that the fusion gene is able to complement Escherichia coli murB and murC temperature sensitive mutants. The purified recombinant fusion enzyme (MurB/CVs) is endowed with UDP-N-acetylmuramate:L-alanine ligase activity. All attempts to demonstrate an in vitro UDP-N-acetylenolpyruvoylglucosamine reductase (MurB) activity are unsuccessful. Phylogenetic analysis reveals that this fusion enzyme can only be identified in specific lineages within the Verrucomicrobia phylum Verrucomicrobium spinosum
metabolism MurB is involved in cytoplasmic steps of peptidoglycan biosynthesis the peptidoglycan biosynthesis pathway, overview Verrucomicrobium spinosum