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Literature summary for 2.7.1.3 extracted from

  • Rangaswamy, V.; Altekar, W.
    Ketohexokinase (ATP:D-fructose 1-phosphotransferase) from a halophilic archaebacterium, Haloarcula vallismortis: purification and properties (1994), J. Bacteriol., 176, 5505-5512.
    View publication on PubMedView publication on EuropePMC

General Stability

General Stability Organism
(NH4)2SO4 stabilizes Haloarcula vallismortis
stabilizing effect of KCl increases with increasing KCl concentration between 0.1 and 2.5 M (ranging from 30 to 98% of the total) Haloarcula vallismortis

Inhibitors

Inhibitors Comment Organism Structure
4-chloromercuribenzoate
-
Haloarcula vallismortis
ADP competitive Haloarcula vallismortis
DTNB
-
Haloarcula vallismortis
LiCl
-
Haloarcula vallismortis
NH4Cl
-
Haloarcula vallismortis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.3
-
ATP pH 9.0, 37°C Haloarcula vallismortis
5
-
D-fructose pH 9.0, 37°C Haloarcula vallismortis

Metals/Ions

Metals/Ions Comment Organism Structure
CsCl the enzyme is maximally active in the presence of 1.2 M KCl. Activity in the presence of RbCl and CsCl is similar to that observed in the presence of KCl Haloarcula vallismortis
KCl the enzyme is maximally active in the presence of 1.2 M KCl. Activity in the presence of RbCl and CsCl is similar to that observed in the presence of KCl Haloarcula vallismortis
Mg2+ most active at a Mg2+ concentration of 1 mM. Mg2+ can not be replaced by Mn2+. ATP/Mg2+ in the ratio of 1:2 forms the actual substrate for ketohexokinase activity Haloarcula vallismortis
NaCl stimulates, yields 50% of the activity observed in equimolar KCl Haloarcula vallismortis
RbCl the enzyme is maximally active in the presence of 1.2 M KCl. Activity in the presence of RbCl and CsCl is similar to that observed in the presence of KCl Haloarcula vallismortis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
95500
-
gel filtration Haloarcula vallismortis
100000
-
sucrose density gradient sedimentation analysis Haloarcula vallismortis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + D-fructose Haloarcula vallismortis
-
ADP + D-fructose 1-phosphate
-
?
ATP + D-fructose Haloarcula vallismortis ATCC 34679
-
ADP + D-fructose 1-phosphate
-
?

Organism

Organism UniProt Comment Textmining
Haloarcula vallismortis
-
-
-
Haloarcula vallismortis ATCC 34679
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Haloarcula vallismortis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + D-fructose
-
Haloarcula vallismortis ADP + D-fructose 1-phosphate
-
?
ATP + D-fructose except for ATP, other nucleotides such as UTP, CTP, GTP, or ITP can not act as phosphoryl donors Haloarcula vallismortis ADP + D-fructose 1-phosphate
-
?
ATP + D-fructose
-
Haloarcula vallismortis ATCC 34679 ADP + D-fructose 1-phosphate
-
?
ATP + D-fructose except for ATP, other nucleotides such as UTP, CTP, GTP, or ITP can not act as phosphoryl donors Haloarcula vallismortis ATCC 34679 ADP + D-fructose 1-phosphate
-
?

Synonyms

Synonyms Comment Organism
ATP:D-fructose 1-phosphotransferase
-
Haloarcula vallismortis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Haloarcula vallismortis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25
-
25°C, 2 h, totally inactivated in 0.1 M KCl/50 mM Tris-HCl (pH 9.0). Stabilizing effect of KCl increases with increasing KCl concentration between 0.1 and 2.5 M (ranging from 30 to 98% of the total). Addition of 50 mM phosphate aids in stabilization of ketohexokinase activity in 0.1 M KCI for about 24 h. Although it is inhibitory for expression of ketohexokinase activity, (NH4)2SO4 stabilizes Haloarcula vallismortis
75
-
30 min, 5% loss of activity Haloarcula vallismortis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
assay at Haloarcula vallismortis

pH Range

pH Minimum pH Maximum Comment Organism
7.5 10.5 activity increases about twofold from pH 7.5 to pH 10.5 Haloarcula vallismortis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.1
-
ADP pH 9.0, 37°C Haloarcula vallismortis
0.2
-
ADP pH 7.5, 37°C Haloarcula vallismortis