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Literature summary extracted from

  • Parikh, A.; Verma, S.K.; Khan, S.; Prakash, B.; Nandicoori, V.K.
    PknB-mediated phosphorylation of a novel substrate, N-acetylglucosamine-1-phosphate uridyltransferase, modulates its acetyltransferase activity (2009), J. Mol. Biol., 386, 451-464.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.157 expressed in Escherichia coli Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.157 crystal structures of GlmU in apo form and UDP-N-acetylglucosamine-bound form is determined. The structure shows a two-domain architecture, with an N-terminal domain having an alpha/beta-like fold and with a C-terminal domain that forms a left-handed parallel beta-helix structure Mycobacterium tuberculosis

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.157 T296A in vitro kinase assays show that the mutant protein is phosphorylated to the same extent as the wild-type GlmU Mycobacterium tuberculosis
2.3.1.157 T308A/T309A/T311A in vitro kinase assays show that the mutant protein is phosphorylated to the same extent as the wild-type GlmU Mycobacterium tuberculosis
2.3.1.157 T324A/T341A/T347A in vitro kinase assays show that the mutant protein is phosphorylated to the same extent as the wild-type GlmU Mycobacterium tuberculosis
2.3.1.157 T365A/T368A/T370A in vitro kinase assays show that the mutant protein is phosphorylated to the same extent as the wild-type GlmU Mycobacterium tuberculosis
2.3.1.157 T376A/T401A/T406A/T407A in vitro kinase assays show that the mutant protein is phosphorylated to the same extent as the wild-type GlmU Mycobacterium tuberculosis
2.3.1.157 T414A/T418A/T425/T432A/T436A in vitro kinase assays show that the mutant protein is not phosphorylated as the wild-type GlmU. These results confine PknB-mediated phosphorylation sites to a smaller region between amino acids 414 and 439 that harbors five threonines Mycobacterium tuberculosis
2.3.1.157 T486A/T494A in vitro kinase assays show that the mutant protein is phosphorylated to the same extent as the wild-type GlmU Mycobacterium tuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.157 0.24
-
 D-glucosamine 1-phosphate Vmax: 4.489 microM/min/pmol enzyme Mycobacterium tuberculosis
2.3.1.157 0.304
-
 acetyl-CoA
-
 Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.157 Mycobacterium tuberculosis
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.3.1.157 phosphoprotein GlmU is a substrate of serine/theronine kinase Pkn B of Mycobacterium tuberculosis and is phosphorylated on threonine residues in region 414-439 in its C-terminal region. PknB-mediated phosphorylation signifcantly decreases the acetyltransferase activity of GlmU Mycobacterium tuberculosis

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
2.3.1.157 homotrimer crystal structure Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
2.3.1.157 GlmU
-
 Mycobacterium tuberculosis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.157 30
-
 assay at Mycobacterium tuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.157 7.6
-
 assay at Mycobacterium tuberculosis