EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
5.3.1.5 | 5-Thio-alpha-D-glucopyranose | competitive | Arthrobacter sp. | |
5.3.1.5 | Ca2+ | strict competitive against Mg2+ | Arthrobacter sp. | |
5.3.1.5 | D-sorbitol | competitive | Arthrobacter sp. |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
5.3.1.5 | 3.3 | - |
D-xylose | D-xylose, with 30 mM Mg2+ | Arthrobacter sp. | |
5.3.1.5 | 110 | - |
D-fructose | with 10-400 mM Mg2+ | Arthrobacter sp. | |
5.3.1.5 | 230 | - |
D-glucose | - |
Arthrobacter sp. | |
5.3.1.5 | 800 | - |
D-fructose | with 1-10 mM Mg2+ | Arthrobacter sp. |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
5.3.1.5 | Co2+ | less effective than Mg2+ in D-fructose isomerization | Arthrobacter sp. | |
5.3.1.5 | Mg2+ | best activator of D-fructose isomerization | Arthrobacter sp. | |
5.3.1.5 | Mn2+ | less effective than Mg2+ in activation of D-fructose isomerization | Arthrobacter sp. |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
5.3.1.5 | Arthrobacter sp. | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.3.1.5 | D-Fructose | compulsory order of binding: 1. Co2+ binds first to site 2 and then to site 1, then the D-fructose binds at site 1. At normal concentrations Mg2+ binds at site 1, then D-fructose, and then Mg2+ at site 2. At very high Mg2+ concentrations, above 10 mM, the order is Mg2+ at site1, Mg2+ at site 2, then D-fructose | Arthrobacter sp. | ? | - |
? | |
5.3.1.5 | D-Glucose | - |
Arthrobacter sp. | D-Fructose | - |
? | |
5.3.1.5 | D-Xylose | - |
Arthrobacter sp. | D-Xylulose | - |
? |