Information on EC 2.4.1.250 - D-inositol-3-phosphate glycosyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.1.250
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RECOMMENDED NAME
GeneOntology No.
D-inositol-3-phosphate glycosyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-D-glucosamine + 1D-myo-inositol 3-phosphate = 1-O-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol 3-phosphate + UDP
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
mycothiol biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-glucosamine:1D-myo-inositol 3-phosphate alpha-D-glycosyltransferase
The enzyme, which belongs to the GT-B fold superfamily, catalyses the first dedicated reaction in the biosynthesis of mycothiol [1]. The substrate was initially believed to be inositol, but eventually shown to be D-myo-inositol 3-phosphate [2]. A substantial conformational change occurs upon UDP binding, which generates the binding site for D-myo-inositol 3-phosphate [3].
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-D-glucosamine + 1D-myo-inositol 1-phosphate
?
show the reaction diagram
UDP-N-acetyl-D-glucosamine + 1D-myo-inositol 3-phosphate
1-O-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol 3-phosphate + UDP
show the reaction diagram
UDP-N-acetyl-D-glucosamine + myo-inositol 2-phosphate
?
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-D-glucosamine + 1D-myo-inositol 3-phosphate
1-O-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol 3-phosphate + UDP
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
1D-myo-inositol 1-phosphate is neither a good substrate nor an inhibitor of MshA. Therefore the commercially available 1DL-myo-inositol 1-phosphate can be used as substrate for MshA assays without complications
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12 - 0.24
1D-myo-inositol 3-phosphate
0.17 - 0.21
UDP-N-acetyl-D-glucosamine
PDB
SCOP
CATH
ORGANISM
UNIPROT
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, 2 weeks, activity in cell extract is stable
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
construction of Mycobacterium tuberculosis with two copies of mshA
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