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Literature summary for 4.2.3.124 extracted from

  • Hirayama, T.; Kudo, F.; Huang, Z.; Eguchi, T.
    Role of glutamate 243 in the active site of 2-deoxy-scyllo-inosose synthase from Bacillus circulans (2007), Bioorg. Med. Chem., 15, 418-423.
    View publication on PubMed
Search for more literature for 4.2.3.124

Protein Variants

Protein Variants Comment Organism
E243Q site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Niallia circulans
K141Q site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Niallia circulans

Inhibitors

Inhibitors Comment Organism Structure
glucose-6-phosphonate
-
 Niallia circulans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady state and pre-steady state kinetic analysis, overview Niallia circulans
0.11
-
 D-glucose 6-phosphate pH 7.7, 37°C, recombinant mutant E243Q Niallia circulans
0.23
-
 D-glucose 6-phosphate pH 7.7, 37°C, recombinant wild-type enzyme Niallia circulans
20
-
 D-glucose 6-phosphate above, pH 7.7, 37°C, recombinant mutant K141Q Niallia circulans

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ required Niallia circulans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glucose 6-phosphate Niallia circulans
-
 2-deoxy-L-scyllo-inosose + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Niallia circulans Q9S5E2 gene btrC
-

Reaction

Reaction Comment Organism Reaction ID
D-glucose 6-phosphate = 2-deoxy-L-scyllo-inosose + phosphate the reaction mechanism includes oxidation of C-4, beta-elimination of phosphate, reduction of C-4, ring opening, and intramolecular aldol cyclization. Completely conserved E243 of BtrC is catalytically involved in the phosphate elimination step Niallia circulans
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose 6-phosphate
-
 Niallia circulans 2-deoxy-L-scyllo-inosose + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
btrC
-
 Niallia circulans
DOI synthase
-
 Niallia circulans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Niallia circulans

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.007
-
 D-glucose 6-phosphate below, pH 7.7, 37°C, recombinant mutant K141Q Niallia circulans
0.017
-
 D-glucose 6-phosphate pH 7.7, 37°C, recombinant mutant E243Q Niallia circulans
0.41
-
 D-glucose 6-phosphate pH 7.7, 37°C, recombinant wild-type enzyme Niallia circulans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.7
-
 assay at Niallia circulans

Cofactor

Cofactor Comment Organism Structure
NAD+ required Niallia circulans

General Information

General Information Comment Organism
additional information the characteristic glutamate residue E243 of DOI synthase is a key determinant to distinguish the reaction mechanism between DOI synthase and dehydroquinate, DHQ, synthase as well as primary sequence, Substrate recognition models of DOI synthase and DHQ synthase, overview Niallia circulans
physiological function 2-deoxy-scyllo-inosose synthase is involved in the biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibiotics and catalyzes the carbocyclic formation from D-glucose 6-phosphate into 2-deoxy-scyllo-inosose Niallia circulans

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.00035
-
 D-glucose 6-phosphate pH 7.7, 37°C, recombinant mutant K141Q Niallia circulans
0.15
-
 D-glucose 6-phosphate pH 7.7, 37°C, recombinant mutant E243Q Niallia circulans
2.4
-
 D-glucose 6-phosphate pH 7.7, 37°C, recombinant wild-type enzyme Niallia circulans