Cloned (Comment) | Organism |
---|---|
overexpression in Escherichia coli | Streptomyces globisporus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.2 | - |
dTTP | - |
Streptomyces globisporus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Co2+ | absolute requirement for a divalent metal ion. Order of effectiveness is: Mn2+, Mg2+, Zn2+, Cu2+, Fe2+, Ni2+, Co2+ | Streptomyces globisporus | |
Cu2+ | absolute requirement for a divalent metal ion. Order of effectiveness is: Mn2+, Mg2+, Zn2+, Cu2+, Fe2+, Ni2+, Co2+ | Streptomyces globisporus | |
Fe2+ | absolute requirement for a divalent metal ion. Order of effectiveness is: Mn2+, Mg2+, Zn2+, Cu2+, Fe2+, Ni2+, Co2+ | Streptomyces globisporus | |
Mg2+ | absolute requirement for a divalent metal ion. Order of effectiveness is: Mn2+, Mg2+, Zn2+, Cu2+, Fe2+, Ni2+, Co2+ | Streptomyces globisporus | |
Mn2+ | absolute requirement for a divalent metal ion. Order of effectiveness is: Mn2+, Mg2+, Zn2+, Cu2+, Fe2+, Ni2+, Co2+ | Streptomyces globisporus | |
Ni2+ | absolute requirement for a divalent metal ion. Order of effectiveness is: Mn2+, Mg2+, Zn2+, Cu2+, Fe2+, Ni2+, Co2+ | Streptomyces globisporus | |
Zn2+ | absolute requirement for a divalent metal ion. Order of effectiveness is: Mn2+, Mg2+, Zn2+, Cu2+, Fe2+, Ni2+, Co2+ | Streptomyces globisporus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
48000 | - |
gel filtration | Streptomyces globisporus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
dTTP + alpha-D-glucose 1-phosphate | Streptomyces globisporus | the enzyme catalyzes the first step in the biosynthesis of 4-deoxy-4-(dimethylamino)-5,5-dimethyl-D-ribopyranose moiety | dTDP-glucose + diphosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Streptomyces globisporus | - |
recombinant | - |
Purification (Comment) | Organism |
---|---|
- |
Streptomyces globisporus |
Storage Stability | Organism |
---|---|
-80 °C, 50 mM potassium phosphate buffer, pH 7.0, containing 1 mM DTT and 20% glycerol, purified SgcA1 is stable for several months with minimal loss of activity | Streptomyces globisporus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
dTTP + alpha-D-glucose 1-phosphate | sequential mechanism | Streptomyces globisporus | dTDP-glucose + diphosphate | - |
? | |
dTTP + alpha-D-glucose 1-phosphate | the enzyme catalyzes the first step in the biosynthesis of 4-deoxy-4-(dimethylamino)-5,5-dimethyl-D-ribopyranose moiety | Streptomyces globisporus | dTDP-glucose + diphosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | - |
Streptomyces globisporus |
Synonyms | Comment | Organism |
---|---|---|
Glc-1-P-TT | - |
Streptomyces globisporus |
SgcA1 | - |
Streptomyces globisporus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2.9 | - |
dTTP | - |
Streptomyces globisporus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | 9 | - |
Streptomyces globisporus |