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Literature summary extracted from

  • Singh, V.K.; Das, K.; Seshadri, K.
    Kinetic modelling of GlmU reactions - prioritization of reaction for therapeutic application (2012), PLoS ONE, 7, e43969.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
2.3.1.157 drug development due to developed resistance against the existing anti-tubercular drugs by Mycobacteriumm tuberculosis, the enzyme is a target for drug development. Targeting uridyltranferase activity of Mtu GlmU would be a better choice for therapeutic intervention, since at low metabolite concentrations, inhibition of either of the GlmU reactions cause significant decrement in the overall GlmU rate, but at higher metabolite concentrations, uridyltransferase inhibition shows higher decrement, overview Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.157 additional information modelling of competitive and uncompetitive inhibition of Rxn-1 by substrates/products, overview Mycobacterium tuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.157 additional information
-
 additional information kinetic modelling of GlmU, simulation of the model, detailed overview. Estimated and measured values are very coherent Mycobacterium tuberculosis
2.3.1.157 0.000009
-
 CoA pH 7.5, 25°C Mycobacterium tuberculosis
2.3.1.157 0.003
-
 N-acetyl-alpha-D-glucosamine 1-phosphate pH 7.5, 25°C Mycobacterium tuberculosis
2.3.1.157 0.061
-
 alpha-D-glucosamine 1-phosphate pH 7.5, 25°C Mycobacterium tuberculosis
2.3.1.157 0.224
-
 acetyl-CoA pH 7.5, 25°C Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.157 acetyl-CoA + alpha-D-glucosamine 1-phosphate Mycobacterium tuberculosis
-
 CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.157 Mycobacterium tuberculosis
-
 gene rxn-1
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.157 acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate both reactions of bifunctional GlmU follow Michaelis Menten ordered bi-bi mechanism involving an obligatory order of binding of substrates to the enzyme Mycobacterium tuberculosis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.157 acetyl-CoA + alpha-D-glucosamine 1-phosphate
-
 Mycobacterium tuberculosis CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 r

Synonyms

EC Number Synonyms Comment Organism
2.3.1.157 GlmU
-
 Mycobacterium tuberculosis
2.3.1.157 glucosamine 1-phosphate N-acetyltransferase/N-acetylglucosamine-1-phosphate uridyltransferase
-
 Mycobacterium tuberculosis
2.3.1.157 Rxn-1
-
 Mycobacterium tuberculosis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.157 25
-
 assay at Mycobacterium tuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.157 7.5
-
 assay at Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
2.3.1.157 physiological function the C- and N-terminal domains of bifunctional enzyme mycobacterial glucosamine 1-phosphate N-acetyltransferase/N-acetylglucosamine-1-phosphate uridyltransferase catalyze acetyltransferase and uridyltransferase (cf. EC 2.7.7.23) activities, respectively, and the final product is involved in peptidoglycan synthesis Mycobacterium tuberculosis