Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.2.3.124 extracted from

  • Kudo, F.; Tamegai, H.; Fujiwara, T.; Tagami, U.; Hirayama, K.; Kakinuma, K.
    Molecular cloning of the gene for the key carbocycle-forming enzyme in the biosynthesis of 2-deoxystreptamine-containing aminocyclitol antibiotics and its comparison with dehydroquinate synthase (1999), J. Antibiot., 52, 559-571.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene btrC, DNA and amino acid sequence determination and analysis, cloning in Escherichia coli strain JM 105, expression in Escherichia coli strain BL21(DE3) Streptomyces fradiae
gene btrC, DNA and amino acid sequence determination and analysis, cloning in Escherichia coli strain JM 105, functional expression in Escherichia coli strain BL21(DE3) Niallia circulans

Inhibitors

Inhibitors Comment Organism Structure
Cu2+
-
Niallia circulans
EDTA complete inhibition Niallia circulans
Ni2+
-
Niallia circulans
Zn2+
-
Niallia circulans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.21
-
D-glucose 6-phosphate pH 7.7, 46°C, recombinant enzyme Niallia circulans

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ required Streptomyces fradiae
Co2+ specifically required Niallia circulans
additional information the enzyme is not affected by Mg2+, Ca2+, Mn2+, and Fe2+ Niallia circulans

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
23000
-
1 * 42000, BtrC, + 1 * 23000, BtrC2, recombinant enzyme, SDS-PAGE, 1 * 40746, BtrC, sequence calculation Niallia circulans
40746
-
1 * 42000, BtrC, + 1 * 23000, BtrC2, recombinant enzyme, SDS-PAGE, 1 * 40746, BtrC, sequence calculation Niallia circulans
42000
-
1 * 42000, BtrC, + 1 * 23000, BtrC2, recombinant enzyme, SDS-PAGE, 1 * 40746, BtrC, sequence calculation Niallia circulans
77000
-
gel filtration, recombinant enzyme Niallia circulans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glucose 6-phosphate Streptomyces fradiae intramolecular carbocyclization, multistep process 2-deoxy-L-scyllo-inosose + phosphate
-
?
D-glucose 6-phosphate Niallia circulans intramolecular carbocyclization, multistep process 2-deoxy-L-scyllo-inosose + phosphate
-
?
D-glucose 6-phosphate Streptomyces fradiae IFO 13147 intramolecular carbocyclization, multistep process 2-deoxy-L-scyllo-inosose + phosphate
-
?
D-glucose 6-phosphate Niallia circulans SANK72073 intramolecular carbocyclization, multistep process 2-deoxy-L-scyllo-inosose + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Niallia circulans Q9S5E2 gene btrC, a butirosin producing strain
-
Niallia circulans SANK72073 Q9S5E2 gene btrC, a butirosin producing strain
-
Streptomyces fradiae
-
gene btrC, a neomycin producing strain
-
Streptomyces fradiae IFO 13147
-
gene btrC, a neomycin producing strain
-

Purification (Commentary)

Purification (Comment) Organism
recombinant BtrC 6.0fold from Escherichia coli strain BL21(DE3) Niallia circulans

Reaction

Reaction Comment Organism Reaction ID
D-glucose 6-phosphate = 2-deoxy-L-scyllo-inosose + phosphate reaction mechanism, overview Streptomyces fradiae
D-glucose 6-phosphate = 2-deoxy-L-scyllo-inosose + phosphate reaction mechanism, overview Niallia circulans

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1
-
purified recombinant BtrC, pH 7.7, 46°C Niallia circulans

Storage Stability

Storage Stability Organism
4°C- -75°C, purified recombinant enzyme, in 50 mM Tris-HCl buffer with 0.2 mM Co2+, loss of 60% activity within 10 days Niallia circulans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose 6-phosphate intramolecular carbocyclization, multistep process Streptomyces fradiae 2-deoxy-L-scyllo-inosose + phosphate
-
?
D-glucose 6-phosphate intramolecular carbocyclization, multistep process Niallia circulans 2-deoxy-L-scyllo-inosose + phosphate
-
?
D-glucose 6-phosphate intramolecular carbocyclization, multistep process Streptomyces fradiae IFO 13147 2-deoxy-L-scyllo-inosose + phosphate
-
?
D-glucose 6-phosphate intramolecular carbocyclization, multistep process Niallia circulans SANK72073 2-deoxy-L-scyllo-inosose + phosphate
-
?

Subunits

Subunits Comment Organism
heterodimer 1 * 42000, BtrC, + 1 * 23000, BtrC2, recombinant enzyme, SDS-PAGE, 1 * 40746, BtrC, sequence calculation Niallia circulans

Synonyms

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
46
-
assay at Streptomyces fradiae
55
-
-
Niallia circulans

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
purified enzyme, pH 7.5-8.5, rapid loss of activity above Niallia circulans

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1
-
D-glucose 6-phosphate pH 7.7, 46°C, recombinant enzyme Niallia circulans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 8.5
-
Niallia circulans
7.7
-
assay at Streptomyces fradiae

Cofactor

Cofactor Comment Organism Structure
NAD+ required, cycling via NADH in the multistep reaction process from D-glucose 6-phosphate to 2-deoxy-L-scyllo-inosose, overview Streptomyces fradiae
NAD+ required, cycling via NADH in the multistep reaction process from D-glucose 6-phosphate to 2-deoxy-L-scyllo-inosose, overview Niallia circulans

General Information

General Information Comment Organism
metabolism the enzyme is involved in the biosynthesis of another major group of classical aminocyclitol antibiotics which contain the 2-deoxystreptamine (DOS) moiety such as neomycin, kanamycin, tobramycin, gentamicin, sisomicin, butirosin, or ribostamycin Streptomyces fradiae
metabolism the enzyme is involved in the biosynthesis of another major group of classical aminocyclitol antibiotics which contain the 2-deoxystreptamine, DOS, moiety such as neomycin, kanamycin, tobramycin, gentamicin, sisomicin, butirosin, or ribostamycin Niallia circulans
physiological function the DOI synthase reaction is a crucial starter step for the biosynthetic pathway of DOS-containing aminocyclitol antibiotics. The DOI synthase catalyzes the intramolecular carbocyclization of D-glucose 6-phosphate into the first non-aminogenous cyclitol 2-deoxy-L-scyllo-inosose, DOI Streptomyces fradiae
physiological function the DOI synthase reaction is a crucial starter step for the biosynthetic pathway of DOS-containing aminocyclitol antibiotics. The DOI synthase catalyzes the intramolecular carbocyclization of D-glucose 6-phosphate into the first non-aminogenous cyclitol 2-deoxy-L-scyllo-inosose, DOI Niallia circulans

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.76
-
D-glucose 6-phosphate pH 7.7, 46°C, recombinant enzyme Niallia circulans