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Literature summary for 5.5.1.4 extracted from

  • Chatterjee, A.; Majee, M.; Ghosh, S.; Majumder, A.L.
    sll1722, an unassigned open reading frame of Synechocystis PCC 6803, codes for L-myo-inositol 1-phosphate synthase (2004), Planta, 218, 989-998.
    View publication on PubMed
Search for more literature for 5.5.1.4

Cloned(Commentary)

Cloned (Comment) Organism
enzyme is encoded by sll1722, an unassigned open reading frame, phylogenetic analysis, subcloning and overexpression in Escherichia coli strains DH5alpha and BL21(DE3) in inclusion bodies Synechocystis sp.

Protein Variants

Protein Variants Comment Organism
additional information the enzyme-deficient Saccharomyces cerevisiae ino1 mutant strain FY250 can be functionally complemented by expression of sll1722 Synechocystis sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.97
-
 D-glucose 6-phosphate pH 7.5, recombinant refolded enzyme Synechocystis sp.
1.19
-
 D-glucose 6-phosphate pH 7.5, native enzyme Synechocystis sp.
1.67
-
 NAD+ pH 7.5, recombinant refolded enzyme Synechocystis sp.
1.95
-
 NAD+ pH 7.5, native enzyme Synechocystis sp.

Metals/Ions

Metals/Ions Comment Organism Structure
NH4+
-
 Synechocystis sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
 x * 50000 + x * 65000, recombinant enzyme form 1, SDS-PAGE Synechocystis sp.
50000
-
 x * 50000 + x * 65000, recombinant enzyme form 2, SDS-PAGE Synechocystis sp.
65000
-
 x * 50000 + x * 65000, recombinant enzyme form 1, SDS-PAGE Synechocystis sp.
65000
-
 x * 50000 + x * 65000, recombinant enzyme form 2, SDS-PAGE Synechocystis sp.
180000
-
 about, recombinant enzyme form 2, gel filtration Synechocystis sp.
200000
-
 about, recombinant enzyme form 1, gel filtration Synechocystis sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-Glucose 6-phosphate Synechocystis sp. first and rate-limiting step in inositol biosynthesis followed by L-myo-inositol 1-phosphate dephosphorylation catalyzed by a Mg2+-dependent inositol 1-phosphatase, EC 3.1.3.25 L-myo-Inositol 1-phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Synechocystis sp.
-
 strain PCC 6803
-

Purification (Commentary)

Purification (Comment) Organism
recombinant, solubilized and refolded enzyme from Escherichia coli strain BL21(DE3) and native enzyme by ion exchange chromatography and gel filtration Synechocystis sp.

Renatured (Commentary)

Renatured (Comment) Organism
solubilization and recvery of about 90% of the recombinant enzyme from inclusion bodies by 8 M urea, refolding in 20 mM Tris-HCl, pH 7.6, 0.5 M NaCl, and 10 mM 2-mercaptoethanol Synechocystis sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.013
-
 purified recombinant refolded enzyme, with cofactor NADP+ Synechocystis sp.
0.015
-
 purified recombinant refolded enzyme, with cofactor NAD+ Synechocystis sp.
0.018
-
 purified native enzyme, with cofactor NADP+ Synechocystis sp.
0.02
-
 purified native enzyme, with cofactor NAD+ Synechocystis sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-Glucose 6-phosphate
-
 Synechocystis sp. L-myo-Inositol 1-phosphate
-
 ?
D-Glucose 6-phosphate first and rate-limiting step in inositol biosynthesis followed by L-myo-inositol 1-phosphate dephosphorylation catalyzed by a Mg2+-dependent inositol 1-phosphatase, EC 3.1.3.25 Synechocystis sp. L-myo-Inositol 1-phosphate
-
 ?

Subunits

Subunits Comment Organism
tetramer x * 50000 + x * 65000, recombinant enzyme form 1, SDS-PAGE Synechocystis sp.
tetramer x * 50000 + x * 65000, recombinant enzyme form 2, SDS-PAGE Synechocystis sp.

Synonyms

Synonyms Comment Organism
L-myo-inositol 1-phosphate synthase
-
 Synechocystis sp.
MIPS
-
 Synechocystis sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Synechocystis sp.

Cofactor

Cofactor Comment Organism Structure
NAD+ slightly preferred cofactor compared to NADP+ Synechocystis sp.
NADP+ almost equally active as NAD+ Synechocystis sp.