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Literature summary for 2.7.1.102 extracted from

  • Beck, E.; Wieczorek, J.; Reinecke, W.
    Purification and properties of hamamelosekinase (1980), Eur. J. Biochem., 107, 485-489.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information enzyme is induced by growing on D-hamamelose Kluyvera cryocrescens

General Stability

General Stability Organism
no stabilization by dithioerythritol, mercaptoethanol, glycerol or bovine serum albumin Kluyvera cryocrescens
purified enzyme is very labile, 4 mM D-hamamelose, added to storage buffer, stabilizes Kluyvera cryocrescens

Inhibitors

Inhibitors Comment Organism Structure
ATP above 7 mM: significant substrate inhibition Kluyvera cryocrescens
hamamelose above 5 mM: significant substrate inhibition Kluyvera cryocrescens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5
-
ATP at 30°C, pH 7.5 Kluyvera cryocrescens
3
-
D-hamamelose at 30°C, pH 7.5 Kluyvera cryocrescens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
21000
-
gel filtration Kluyvera cryocrescens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + D-hamamelose Kluyvera cryocrescens initial step of the catabolic reaction sequence for dissimilation of hamamelose ADP + hamamelose 2'-phosphate
-
?
ATP + D-hamamelose Kluyvera cryocrescens 627 initial step of the catabolic reaction sequence for dissimilation of hamamelose ADP + hamamelose 2'-phosphate
-
?

Organism

Organism UniProt Comment Textmining
Kluyvera cryocrescens
-
grown on D-hamamelose
-
Kluyvera cryocrescens 627
-
grown on D-hamamelose
-

Purification (Commentary)

Purification (Comment) Organism
partial, 51fold Kluyvera cryocrescens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.6 6.6 at 30°C, pH 7.5 Kluyvera cryocrescens

Storage Stability

Storage Stability Organism
-20°C, purified enzyme, within 10 days, complete loss of activity Kluyvera cryocrescens
low temperatures, 4 mM hamamelose, protein concentration not lower than 0.2 mg/ml, stable Kluyvera cryocrescens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + D-hamamelitol poor substrate Kluyvera cryocrescens ADP + D-hamamelitol 2'-phosphate
-
?
ATP + D-hamamelitol poor substrate Kluyvera cryocrescens 627 ADP + D-hamamelitol 2'-phosphate
-
?
ATP + D-hamamelose specific for hamamelose Kluyvera cryocrescens ADP + hamamelose 2'-phosphate
-
?
ATP + D-hamamelose initial step of the catabolic reaction sequence for dissimilation of hamamelose Kluyvera cryocrescens ADP + hamamelose 2'-phosphate
-
?
ATP + D-hamamelose specific for hamamelose Kluyvera cryocrescens 627 ADP + hamamelose 2'-phosphate
-
?
ATP + D-hamamelose initial step of the catabolic reaction sequence for dissimilation of hamamelose Kluyvera cryocrescens 627 ADP + hamamelose 2'-phosphate
-
?
additional information no substrates: D-glucose, D-glucosamine, D-fructose, D-mannose, D-galactose, D-arabinose, D-xylose Kluyvera cryocrescens ?
-
?
additional information no substrates: D-glucose, D-glucosamine, D-fructose, D-mannose, D-galactose, D-arabinose, D-xylose Kluyvera cryocrescens 627 ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Kluyvera cryocrescens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Kluyvera cryocrescens

pH Range

pH Minimum pH Maximum Comment Organism
6.6 8.5 10% of maximal activity at pH 6.6, 80% of maximal activity at pH 8.5 Kluyvera cryocrescens

pH Stability

pH Stability pH Stability Maximum Comment Organism
6.4
-
optimal enzyme stability in the crude extract at Kluyvera cryocrescens