Literature summary for 2.3.1.157 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.

Search for more literature for 2.3.1.157

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli	Mycobacterium tuberculosis

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Protein Variants	Comment	Organism
T296A	in vitro kinase assays show that the mutant protein is phosphorylated to the same extent as the wild-type GlmU	Mycobacterium tuberculosis
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
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
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
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
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
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]

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

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
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)

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

Subunits

Subunits	Comment	Organism
homotrimer	crystal structure	Mycobacterium tuberculosis

Synonyms

Synonyms	Comment	Organism
GlmU	-	Mycobacterium tuberculosis

Temperature Optimum [°C]

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

pH Optimum

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

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Release 2023.1 (January 2023)