4.2.3.124: 2-deoxy-scyllo-inosose synthase
This is an abbreviated version!
For detailed information about 2-deoxy-scyllo-inosose synthase, go to the full flat file.
Word Map on EC 4.2.3.124
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4.2.3.124
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aminoglycoside
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circulans
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2-deoxystreptamine-containing
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2-deoxystreptamine
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carbocycle
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butirosin
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aminocyclitols
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dehydroquinate
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butirosin-producing
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aglycon
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kanamycin
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neomycin
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tobramycin
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actinomycete
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gentamicin
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nad+
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catechol
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tenebrarius
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cyclization
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micromonospora
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amacs
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aminoglycoside-aminocyclitols
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benzenoid
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shikimate
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industry
- 4.2.3.124
- aminoglycoside
- circulans
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2-deoxystreptamine-containing
- 2-deoxystreptamine
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carbocycle
- butirosin
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aminocyclitols
- dehydroquinate
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butirosin-producing
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aglycon
- kanamycin
- neomycin
- tobramycin
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actinomycete
- gentamicin
- nad+
- catechol
- tenebrarius
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cyclization
- micromonospora
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amacs
- aminoglycoside-aminocyclitols
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benzenoid
- shikimate
- industry
Reaction
Synonyms
AlloH, btrC, BtrC2, DOI synthase, DOIS, KanA, kanC, neoC, tbmA
ECTree
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General Information
General Information on EC 4.2.3.124 - 2-deoxy-scyllo-inosose synthase
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evolution
malfunction
metabolism
physiological function
additional information
2-deoxy-scyllo-inosose synthase, i.e. DOIS or BtrC, clearly belongs to the family of dehydroquinate synthase, DHQS
evolution
evolutionary relationship between dehydroquinate synthase and 2-deoxy-scyllo-inosose synthase, overview
disruption of gene btrC2 reduces the growth rate and antibiotics production, the growth rate is restored by addition of NH4Cl, both by addition of yeast extract
malfunction
Niallia circulans SANK72073
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disruption of gene btrC2 reduces the growth rate and antibiotics production, the growth rate is restored by addition of NH4Cl, both by addition of yeast extract
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2-deoxy-scyllo-inosose synthase is the starter enzyme for 2-deoxystreptamine biosynthesis. 2-Deoxystreptamine is the aglycon of clinically important aminocyclitol antibiotics
metabolism
2-deoxy-scyllo-inosose synthase, DOIS, is a key enzyme in the biosynthesis of 2-deoxystreptamine-containing aminocyclitol antibiotics
metabolism
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DOI synthase is a key enzyme in the biosynthesis of 2-deoxy-scyllo-inosose, DOS
metabolism
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DOI synthase is a key enzyme in the biosynthesis of 2-deoxy-scyllo-inosose, DOS
metabolism
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DOI synthase is a key enzyme in the biosynthesis of 2-deoxy-scyllo-inosose, DOS
metabolism
DOI synthase is the key starter enzyme of 2-deoxystreptamine biosynthesis
metabolism
key enzyme in the biosynthesis of 2-deoxystreptamine-containing aminocyclitol antibiotics
metabolism
key enzyme in the biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibiotics. Multistep cyclization of D-glucose-6-phosphate into the six-membered carbocycle 2-deoxy-L-scyllo-inosose is the first step of 2-deoxystreptamine biosynthesis
metabolism
key enzyme in the biosynthesis of 2-deoxytstreptamine. The function od BtrC2 in biosynthesis of butirosin is indirect. BtrC2 is involved in secondary as well as primary metabolism probably playing a role in stabilizing and regulating DOI synthase
metabolism
key enzyme in the biosynthesis of clinically important aminoglycoside antibiotics is 2-deoxy-scyllo-inosose synthase, which catalyzes carbocycle formation from D-glucose 6-phosphate to 2-deoxy-scyllo-inosose through a multistep reaction
metabolism
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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
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
metabolism
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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
metabolism
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DOI synthase is a key enzyme in the biosynthesis of 2-deoxy-scyllo-inosose, DOS
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metabolism
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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
-
metabolism
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DOI synthase is a key enzyme in the biosynthesis of 2-deoxy-scyllo-inosose, DOS
-
metabolism
-
DOI synthase is a key enzyme in the biosynthesis of 2-deoxy-scyllo-inosose, DOS
-
metabolism
Niallia circulans SANK72073
-
2-deoxy-scyllo-inosose synthase is the starter enzyme for 2-deoxystreptamine biosynthesis. 2-Deoxystreptamine is the aglycon of clinically important aminocyclitol antibiotics
-
metabolism
Niallia circulans SANK72073
-
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
-
metabolism
Niallia circulans SANK72073
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key enzyme in the biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibiotics. Multistep cyclization of D-glucose-6-phosphate into the six-membered carbocycle 2-deoxy-L-scyllo-inosose is the first step of 2-deoxystreptamine biosynthesis
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metabolism
Niallia circulans SANK72073
-
2-deoxy-scyllo-inosose synthase, DOIS, is a key enzyme in the biosynthesis of 2-deoxystreptamine-containing aminocyclitol antibiotics
-
metabolism
Niallia circulans SANK72073
-
key enzyme in the biosynthesis of clinically important aminoglycoside antibiotics is 2-deoxy-scyllo-inosose synthase, which catalyzes carbocycle formation from D-glucose 6-phosphate to 2-deoxy-scyllo-inosose through a multistep reaction
-
metabolism
Niallia circulans SANK72073
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key enzyme in the biosynthesis of 2-deoxytstreptamine. The function od BtrC2 in biosynthesis of butirosin is indirect. BtrC2 is involved in secondary as well as primary metabolism probably playing a role in stabilizing and regulating DOI synthase
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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
physiological function
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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
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
physiological function
the enzyme is crucial in the carbocyclization reaction as part of the biosynthesis of 2-deoxystreptamine-containing aminoglycoside 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
physiological function
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the enzyme is crucial in the carbocyclization reaction as part of the biosynthesis of 2-deoxystreptamine-containing aminoglycoside 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
physiological function
the role of the 20 kDa non-catalytic protein BtrC2, associated with the DOI synthase, in butirosin biosynthesis is to stabilize the synthase by complexing as heterodimer with BtrC allowing the stable production of butirosin for long periods. BtrC2 is also involved in the biosynthesis of vitamin B6 in primary metabolism
physiological function
2-deoxy-scyllo-inosose (DOI) synthase, which uses glucose-6-phosphate as a substrate for DOI biosynthesis, is indispensably involved in the initial stage of the biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibiotics including butirosin, gentamicin, kanamycin, and tobramycin
physiological function
2-deoxy-scyllo-inosose (DOI) synthase, which uses glucose-6-phosphate as a substrate for DOI biosynthesis, is indispensably involved in the initial stage of the biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibiotics including butirosin, gentamicin, kanamycin, and tobramycin
physiological function
DOI synthase (DOIS) is responsible for the formation of DOI from D-glucose-6-phosphate in the biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibiotics such as neomycin and butirosin
physiological function
-
2-deoxy-scyllo-inosose (DOI) synthase, which uses glucose-6-phosphate as a substrate for DOI biosynthesis, is indispensably involved in the initial stage of the biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibiotics including butirosin, gentamicin, kanamycin, and tobramycin
-
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
-
physiological function
Niallia circulans SANK72073
-
the enzyme is crucial in the carbocyclization reaction as part of the biosynthesis of 2-deoxystreptamine-containing aminoglycoside 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
-
physiological function
Niallia circulans SANK72073
-
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
-
physiological function
Niallia circulans SANK72073
-
the role of the 20 kDa non-catalytic protein BtrC2, associated with the DOI synthase, in butirosin biosynthesis is to stabilize the synthase by complexing as heterodimer with BtrC allowing the stable production of butirosin for long periods. BtrC2 is also involved in the biosynthesis of vitamin B6 in primary metabolism
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active site structure is located between the N-terminal and C-terminal domains. Two subunits exist as a dimer in the asymmetric unit. The two active sites of the dimer are different. One contains a dephosphorylated compound derived from the inhibitor and the other includes the inhibitor without change. Comparison of active site between the native and complex BtrC, overview
additional information
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active site structure is located between the N-terminal and C-terminal domains. Two subunits exist as a dimer in the asymmetric unit. The two active sites of the dimer are different. One contains a dephosphorylated compound derived from the inhibitor and the other includes the inhibitor without change. Comparison of active site between the native and complex BtrC, overview
additional information
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Streptoalloteichus hindustanus seems to have two sets of DOS-containing antibiotic biosynthetic gene cluster for tobramycin and apramycin
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
additional information
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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
additional information
while the reaction mechanisms are quite similar, 2-deoxy-scyllo-inosose synthase is distinct from 3-dehydroquinate synthase, EC 4.2.3.4, in the shikimate pathway, with respect to the quaternary structure, metal ion requirement, and the kinetic parameters
additional information
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while the reaction mechanisms are quite similar, 2-deoxy-scyllo-inosose synthase is distinct from 3-dehydroquinate synthase, EC 4.2.3.4, in the shikimate pathway, with respect to the quaternary structure, metal ion requirement, and the kinetic parameters
additional information
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Streptoalloteichus hindustanus seems to have two sets of DOS-containing antibiotic biosynthetic gene cluster for tobramycin and apramycin
-
additional information
Niallia circulans SANK72073
-
while the reaction mechanisms are quite similar, 2-deoxy-scyllo-inosose synthase is distinct from 3-dehydroquinate synthase, EC 4.2.3.4, in the shikimate pathway, with respect to the quaternary structure, metal ion requirement, and the kinetic parameters
-
additional information
Niallia circulans SANK72073
-
active site structure is located between the N-terminal and C-terminal domains. Two subunits exist as a dimer in the asymmetric unit. The two active sites of the dimer are different. One contains a dephosphorylated compound derived from the inhibitor and the other includes the inhibitor without change. Comparison of active site between the native and complex BtrC, overview
-