Inhibitors | Comment | Organism | Structure |
---|---|---|---|
D-mannose | competitive to D-glucose; glucokinase | Saccharomyces cerevisiae | |
D-xylose | irreversible inactivation of the 3 isoenzymes, hexokinase PI inactivation requires ATP, hexokinase PII is inactivated by D-xylose without ATP, glucokinase is protected by ATP, competitive inhibitor of hexokinase PI and glucokinase, non-competitive inhibitor of hexokinase PII | Saccharomyces cerevisiae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | - |
Saccharomyces cerevisiae | |
0.04 | - |
D-glucose | glucokinase | Saccharomyces cerevisiae | |
0.04 | - |
D-mannose | glucokinase | Saccharomyces cerevisiae | |
0.12 | - |
D-glucose | hexokinases PI and PII | Saccharomyces cerevisiae | |
0.33 | - |
D-fructose | hexokinases PI and PII | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Saccharomyces cerevisiae | hexokinase PI is a constitutive enzyme, hexokinase PII and glucokinase are regulated by the carbon source used | ? | - |
? | |
additional information | Saccharomyces cerevisiae G-517 / CECT 1317 | hexokinase PI is a constitutive enzyme, hexokinase PII and glucokinase are regulated by the carbon source used | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
3 isoenzymes PI, PII and glucokinase | - |
Saccharomyces cerevisiae G-517 / CECT 1317 | - |
3 isoenzymes PI, PII and glucokinase | - |
Purification (Comment) | Organism |
---|---|
3 isoenzymes PI, PII and glucokinase, partial | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-fructose + ATP | hexokinases PI and PII phosphorylate fructose 2.5 and 1.5times faster than glucose, glucokinase: very low or no activity | Saccharomyces cerevisiae | ADP + D-fructose 6-phosphate | - |
? | |
D-fructose + ATP | hexokinases PI and PII phosphorylate fructose 2.5 and 1.5times faster than glucose, glucokinase: very low or no activity | Saccharomyces cerevisiae G-517 / CECT 1317 | ADP + D-fructose 6-phosphate | - |
? | |
D-glucose + ATP | - |
Saccharomyces cerevisiae | ADP + D-glucose 6-phosphate | - |
? | |
D-glucose + ATP | - |
Saccharomyces cerevisiae G-517 / CECT 1317 | ADP + D-glucose 6-phosphate | - |
? | |
D-mannose + ATP | glucokinase | Saccharomyces cerevisiae | ADP + D-mannose 6-phosphate | - |
? | |
D-mannose + ATP | glucokinase | Saccharomyces cerevisiae G-517 / CECT 1317 | ADP + D-mannose 6-phosphate | - |
? | |
additional information | glucokinase: not: fructose, galactose, sorbose, rhamnose, arabinose, mannitol, sorbitol, ribose | Saccharomyces cerevisiae | ? | - |
? | |
additional information | hexokinase PI is a constitutive enzyme, hexokinase PII and glucokinase are regulated by the carbon source used | Saccharomyces cerevisiae | ? | - |
? | |
additional information | glucokinase: not: fructose, galactose, sorbose, rhamnose, arabinose, mannitol, sorbitol, ribose | Saccharomyces cerevisiae G-517 / CECT 1317 | ? | - |
? | |
additional information | hexokinase PI is a constitutive enzyme, hexokinase PII and glucokinase are regulated by the carbon source used | Saccharomyces cerevisiae G-517 / CECT 1317 | ? | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Saccharomyces cerevisiae |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.06 | - |
D-mannose | glucokinase | Saccharomyces cerevisiae | |
0.85 | - |
D-xylose | glucokinase | Saccharomyces cerevisiae | |
25 | - |
D-xylose | hexokinase PI | Saccharomyces cerevisiae | |
80 | - |
D-xylose | hexokinase PII | Saccharomyces cerevisiae |