Literature summary for 2.4.1.250 extracted from

Vetting, M.W.; Frantom, P.A.; Blanchard, J.S.
Structural and enzymatic analysis of MshA from Corynebacterium glutamicum: substrate-assisted catalysis (2008), J. Biol. Chem., 283, 15834-15844.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Corynebacterium glutamicum

Crystallization (Commentary)

Crystallization (Comment)	Organism
vapor diffusion under silicon oil. The structure of MshA is determined both in the absence of substrates and in a complex with UDP and 11D-myo-inositol 3-phosphate. The structure of unliganded CgMshA (APO form) is determined by single isomorphous replacement with anomalous scattering utilizing a CuKalpha home source and a mercury derivative to 2.1 A resolution. Crystallization of CgMshA in the presence of UDP or UDP-GlcNAc results in a tetragonal crystal form. The structure of MshA from Corynebacterium glutamicum is determined both in the absence of substrates and in a complex with UDP and 1L-myo-inositol-1-phosphate	Corynebacterium glutamicum

Crystallization (Comment)

Organism

vapor diffusion under silicon oil. The structure of MshA is determined both in the absence of substrates and in a complex with UDP and 11D-myo-inositol 3-phosphate. The structure of unliganded CgMshA (APO form) is determined by single isomorphous replacement with anomalous scattering utilizing a CuKalpha home source and a mercury derivative to 2.1 A resolution. Crystallization of CgMshA in the presence of UDP or UDP-GlcNAc results in a tetragonal crystal form. The structure of MshA from Corynebacterium glutamicum is determined both in the absence of substrates and in a complex with UDP and 1L-myo-inositol-1-phosphate

Corynebacterium glutamicum

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.21	-	UDP-N-acetyl-D-glucosamine	pH 7.8, 25°C	Corynebacterium glutamicum
0.24	-	1D-myo-inositol 3-phosphate	pH 7.8, 25°C	Corynebacterium glutamicum

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
UDP-N-acetyl-D-glucosamine + 1D-myo-inositol 3-phosphate	Corynebacterium glutamicum	1D-myo-inositol 3-phosphate i.e. 1L-myo-inositol 1-phosphate, committed step of mycothiol biosynthesis	1-O-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol 3-phosphate + UDP	-	?

Organism

Organism	UniProt	Comment	Textmining
Corynebacterium glutamicum	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Corynebacterium glutamicum

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
UDP-N-acetyl-D-glucosamine + 1D-myo-inositol 3-phosphate	1D-myo-inositol 3-phosphate i.e. 1L-myo-inositol 1-phosphate, committed step of mycothiol biosynthesis	Corynebacterium glutamicum	1-O-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol 3-phosphate + UDP	-	?
UDP-N-acetyl-D-glucosamine + 1D-myo-inositol 3-phosphate	1D-myo-inositol 3-phosphate i.e. 1L-myo-inositol 1-phosphate. Molecular models of the ternary complex suggest a mechanism in which the beta-phosphate of the substrate, UDP-N-acetylglucosamine, promotes the nucleophilic attack of the 3-hydroxyl group of 1D-myo-inositol 3-phosphate while at the same time promoting the cleavage of the sugar nucleotide bond	Corynebacterium glutamicum	1-O-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol 3-phosphate + UDP	-	?

Synonyms

Synonyms	Comment	Organism
CgMshA	-	Corynebacterium glutamicum