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Literature summary for 2.7.1.1 extracted from

  • Herrero, R.F.P.; Moreno, F.
    Inhibition and inactivation of glucose-phosphorylating enzymes from Saccharomyces cerevisiae by D-xylose (1985), J. Gen. Microbiol., 131, 2705-2709.
    View publication on PubMed

Inhibitors

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 [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/ Products (Substrates)

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

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 (Commentary)

Purification (Comment) Organism
3 isoenzymes PI, PII and glucokinase, partial Saccharomyces cerevisiae

Substrates and Products (Substrate)

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 [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
ATP
-
Saccharomyces cerevisiae

Ki Value [mM]

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