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Literature summary 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 PubMed

General Stability

EC Number General Stability Organism
2.7.1.3 (NH4)2SO4 stabilizes Haloarcula vallismortis
2.7.1.3 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

EC Number Inhibitors Comment Organism Structure
2.7.1.3 4-chloromercuribenzoate
-
 Haloarcula vallismortis
2.7.1.3 ADP competitive Haloarcula vallismortis
2.7.1.3 DTNB
-
 Haloarcula vallismortis
2.7.1.3 LiCl
-
 Haloarcula vallismortis
2.7.1.3 NH4Cl
-
 Haloarcula vallismortis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.3 3.3
-
 ATP pH 9.0, 37°C Haloarcula vallismortis
2.7.1.3 5
-
 D-fructose pH 9.0, 37°C Haloarcula vallismortis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.3 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
2.7.1.3 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
2.7.1.3 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
2.7.1.3 NaCl stimulates, yields 50% of the activity observed in equimolar KCl Haloarcula vallismortis
2.7.1.3 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.1.3 95500
-
 gel filtration Haloarcula vallismortis
2.7.1.3 100000
-
 sucrose density gradient sedimentation analysis Haloarcula vallismortis

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.3 Haloarcula vallismortis
-
-
-
2.7.1.3 Haloarcula vallismortis ATCC 34679
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.3
-
 Haloarcula vallismortis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.3 ATP + D-fructose
-
 Haloarcula vallismortis ADP + D-fructose 1-phosphate
-
 ?
2.7.1.3 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
-
 ?
2.7.1.3 ATP + D-fructose
-
 Haloarcula vallismortis ATCC 34679 ADP + D-fructose 1-phosphate
-
 ?
2.7.1.3 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

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.1.3 37
-
 assay at Haloarcula vallismortis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.1.3 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
2.7.1.3 75
-
 30 min, 5% loss of activity Haloarcula vallismortis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.1.3 9
-
 assay at Haloarcula vallismortis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.7.1.3 7.5 10.5 activity increases about twofold from pH 7.5 to pH 10.5 Haloarcula vallismortis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.1.3 0.1
-
 ADP pH 9.0, 37°C Haloarcula vallismortis
2.7.1.3 0.2
-
 ADP pH 7.5, 37°C Haloarcula vallismortis