Literature summary for 5.5.1.4 extracted from

Jin, X.; Foley, K.M.; Geiger, J.H.
The structure of the 1L-myo-inositol 1-phosphate synthase/NAD+ /2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate complex demands a revision of the enzyme's mechanism (2004), J. Biol. Chem., 279, 13889-13895.

Search for more literature for 5.5.1.4

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified apo-enzyme and in complex with NAD+ and 2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate, complexing by soaking of apo-enzyme crystals in 5% PEG 8000, 0.1 M NaAc, pH 5.5, 1 mM NAD+, and 13.5 mM 2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate for 24 h, cryoprotection by 30% glycerol, X-ray diffraction structure determination and analysis at 2.0 A resolution	Saccharomyces cerevisiae
structure of the 1L-myo-inositol 1-phosphate synthase/NAD+/2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate complex	Saccharomyces cerevisiae

Protein Variants

Protein Variants	Comment	Organism
K369A	mutation results in complete loss of activity	Saccharomyces cerevisiae
K369A	site-directed mutagenesis, mutant shows altered substrate and inhibitor binding	Saccharomyces cerevisiae
K412A	mutation results in complete loss of activity	Saccharomyces cerevisiae
K412A	site-directed mutagenesis, mutant shows altered substrate and inhibitor binding	Saccharomyces cerevisiae
K489A	mutation results in complete loss of activity	Saccharomyces cerevisiae
K489A	site-directed mutagenesis, mutant shows altered substrate and inhibitor binding	Saccharomyces cerevisiae

Inhibitors

Inhibitors	Comment	Organism	Structure
2-deoxy-D-glucitol	-	Saccharomyces cerevisiae
2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate	binding structure, interaction with active site residues, overview	Saccharomyces cerevisiae

Metals/Ions

Metals/Ions	Comment	Organism	Structure
NH4+	-	Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
D-glucose 6-phosphate	Saccharomyces cerevisiae	the enzyme catalyzes the first and rate-limiting step in biosynthesis of inositol-containg compounds	1D-inositol 3-phosphate	-	?
D-glucose 6-phosphate	Saccharomyces cerevisiae	first and rate-limiting step in biosynthesis of all inositol-conatining compounds	1L-myo-inositol 1-phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate	catalytic reaction mechanism involving K369, K412, K373, and K489	Saccharomyces cerevisiae	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-glucose 6-phosphate	the enzyme catalyzes the first and rate-limiting step in biosynthesis of inositol-containg compounds	Saccharomyces cerevisiae	1D-inositol 3-phosphate	-	?
D-glucose 6-phosphate	first and rate-limiting step in biosynthesis of all inositol-conatining compounds	Saccharomyces cerevisiae	1L-myo-inositol 1-phosphate	-	?
D-glucose 6-phosphate	determination of the catalytic reaction mechanism	Saccharomyces cerevisiae	1L-myo-inositol 1-phosphate	-	?

Subunits

Subunits	Comment	Organism
More	structure of the enzyme-NAD+-2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate complex	Saccharomyces cerevisiae

Synonyms

Synonyms	Comment	Organism
1L-myo-Inositol-1-phosphate synthase	-	Saccharomyces cerevisiae
MIP synthase	-	Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.7	-	assay at	Saccharomyces cerevisiae

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Saccharomyces cerevisiae

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.00067	-	2-deoxy-D-glucitol	pH 5.5	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)