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Literature summary extracted from

  • Mukai, T.; Kawai, S.; Matsukawa, H.; Matuo, Y.; Murata, K.
    Characterization and molecular cloning of a novel enzyme, inorganic polyphosphate/ATP-glucomannokinase, of Arthrobacter sp. strain KM (2003), Appl. Environ. Microbiol., 69, 3849-3857.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.1.7 Polyphosphate dependent on, can be substituted by ATP, nonprocessive utilization, binding site is the same as for ATP binding Arthrobacter sp.

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.7 DNA and amino acid sequence determination and analysis, phylogenetic analysis Arthrobacter sp.
2.7.1.63
-
 Arthrobacter sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.7 0.02
-
 Hexametaphosphate pH 7.0 Arthrobacter sp.
2.7.1.7 0.2
-
 ATP pH 7.0 Arthrobacter sp.
2.7.1.7 0.5
-
 D-glucose pH 7.0 Arthrobacter sp.
2.7.1.7 15
-
 D-mannose pH 7.0 Arthrobacter sp.
2.7.1.63 0.02
-
 Hexametaphosphate pH 7.0, 30°C Arthrobacter sp.
2.7.1.63 0.15
-
 mannose pH 7.0, 30°C Arthrobacter sp.
2.7.1.63 0.2
-
 ATP pH 7.0, 30°C Arthrobacter sp.
2.7.1.63 0.5
-
 glucose pH 7.0, 30°C Arthrobacter sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.7 Co2+ activates, 86% and 30% activity with polyphosphate and ATP, respectively, compared to Mg2+ Arthrobacter sp.
2.7.1.7 Cu2+ activates, 11% activity with polyphosphate compared to Mg2+, no activity with ATP Arthrobacter sp.
2.7.1.7 Fe2+ activates, 15% activity with ATP compared to Mg2+, no activity with polyphosphate Arthrobacter sp.
2.7.1.7 Mg2+ absolutely required, most effective metal ion Arthrobacter sp.
2.7.1.7 Mn2+ activates, 82% and 88% activity with polyphosphate and ATP, respectively, compared to Mg2+ Arthrobacter sp.
2.7.1.7 additional information activities with different divalent cations in descending order: Mg2+, Mn2+, Co2+, Zn2+, Cu2+, and Fe2+, no activity with Hg2+ Arthrobacter sp.
2.7.1.7 Zn2+ activates, 80% and 19% activity with polyphosphate and ATP, respectively, compared to Mg2+ Arthrobacter sp.
2.7.1.63 Co2+ divalent cation required, 86% of the activity with Mg2+ for the polyphosphate-dependent activity and 30% of the activity with Mg2+ for ATP-dependent activity, 5 mM Arthrobacter sp.
2.7.1.63 Cu2+ divalent cation required, 11% of the activity with Mg2+ for the polyphosphate-dependent activity and no activation of ATP-dependent activity, 5 mM Arthrobacter sp.
2.7.1.63 Fe2+ divalent cation required, no activation of the polyphosphate-dependent activity and 15% of the activity with Mg2+ for ATP-dependent acticity, 5 mM Arthrobacter sp.
2.7.1.63 Mg2+ divalent cation required, maximal activition of polyphosphate-dependent glucokinase and ATP-dependent glucokinase activity, 5 mM Arthrobacter sp.
2.7.1.63 Mn2+ divalent cation required, 82% of the activity with Mg2+ for the polyphosphate-dependent activity and 88% of the activity with Mg2+ for ATP-dependent activity, 5 mM Arthrobacter sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.1.7 30000
-
-
 Arthrobacter sp.

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.7 Arthrobacter sp. Q7WT42
-
-
2.7.1.7 Arthrobacter sp. KM Q7WT42
-
-
2.7.1.63 Arthrobacter sp.
-
-
-
2.7.1.63 Arthrobacter sp. KM
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.7 native enzyme 2200fold and 1375fold determined with polyphosphate and ATP, respectively, to homogeneity Arthrobacter sp.
2.7.1.63
-
 Arthrobacter sp.

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.1.7 ATP + D-mannose = ADP + D-mannose 6-phosphate mechanism, enzyme shows both mannokinase and glucokinase activities Arthrobacter sp.
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.1.7 0.064
-
 mannokinase activity with polyphosphate in cell extract Arthrobacter sp.
2.7.1.7 0.077
-
 mannokinase activity with ATP in cell extract Arthrobacter sp.
2.7.1.7 110
-
 purified enzyme, mannokinase activity with ATP Arthrobacter sp.
2.7.1.7 220
-
 purified enzyme, mannokinase activity with polyphosphate Arthrobacter sp.
2.7.1.63 110
-
 reaction with ATP and glucose Arthrobacter sp.
2.7.1.63 220
-
 reaction with polyphosphate and glucose Arthrobacter sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.7 ATP + D-glucose
-
 Arthrobacter sp. ADP + D-glucose 6-phosphate
-
 ?
2.7.1.7 ATP + D-glucose
-
 Arthrobacter sp. KM ADP + D-glucose 6-phosphate
-
 ?
2.7.1.7 ATP + D-mannose
-
 Arthrobacter sp. ADP + D-mannose 6-phosphate
-
 ?
2.7.1.7 ATP + D-mannose
-
 Arthrobacter sp. KM ADP + D-mannose 6-phosphate
-
 ?
2.7.1.7 hexametaphosphate + D-mannose
-
 Arthrobacter sp. pentaphosphate + D-mannose 6-phosphate
-
 ?
2.7.1.7 hexametaphosphate + D-mannose
-
 Arthrobacter sp. KM pentaphosphate + D-mannose 6-phosphate
-
 ?
2.7.1.7 additional information enzyme is also active with D-glucose, which is a more efficient substrate than D-mannose, ratio 3:2 and 3:1 with ATP and polyphosphate, respectively Arthrobacter sp. ?
-
 ?
2.7.1.7 additional information enzyme is also active with D-glucose, which is a more efficient substrate than D-mannose, ratio 3:2 and 3:1 with ATP and polyphosphate, respectively Arthrobacter sp. KM ?
-
 ?
2.7.1.63 (phosphate)n + D-glucose
-
 Arthrobacter sp. (phosphate)n-1 + D-glucose 6-phosphate
-
 ir
2.7.1.63 (phosphate)n + D-glucose
-
 Arthrobacter sp. KM (phosphate)n-1 + D-glucose 6-phosphate
-
 ir
2.7.1.63 (phosphate)n + D-mannose about 40% of the activity with glucose Arthrobacter sp. (phosphate)n-1 + D-mannose 6-phosphate
-
 ?
2.7.1.63 (phosphate)n + D-mannose about 40% of the activity with glucose Arthrobacter sp. KM (phosphate)n-1 + D-mannose 6-phosphate
-
 ?
2.7.1.63 ATP + D-glucose
-
 Arthrobacter sp. ADP + D-glucose 6-phosphate
-
 ?
2.7.1.63 ATP + D-glucose
-
 Arthrobacter sp. KM ADP + D-glucose 6-phosphate
-
 ?
2.7.1.63 ATP + D-mannose about 30% of the activity with glucose Arthrobacter sp. ADP + D-mannose 6-phosphate
-
 ?
2.7.1.63 ATP + D-mannose about 30% of the activity with glucose Arthrobacter sp. KM ADP + D-mannose 6-phosphate
-
 ?
2.7.1.63 hexametaphosphate + D-glucose
-
 Arthrobacter sp. pentametaphosphate + D-glucose 6-phosphate
-
 ?
2.7.1.63 additional information the enzyme also shows weak NAD kinase activity and fructokinase activity with polyphosphate or ATP Arthrobacter sp. ?
-
 ?
2.7.1.63 additional information the enzyme also shows weak NAD kinase activity and fructokinase activity with polyphosphate or ATP Arthrobacter sp. KM ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.1.7 monomer 1 * 30000 Arthrobacter sp.

Synonyms

EC Number Synonyms Comment Organism
2.7.1.7 inorganic polyphosphate/ATP-glucomannokinase
-
 Arthrobacter sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.1.7 45
-
-
 Arthrobacter sp.
2.7.1.63 45
-
 polyphosphate-dependent and ATP-dependent mannokinase activity, polyphosphate and ATP-dependent glucokinase activity Arthrobacter sp.

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.1.7 40
-
 loss of 50% activity after 5 min Arthrobacter sp.
2.7.1.63 40
-
 5 min, 50% loss of activity Arthrobacter sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.1.7 7.5
-
-
 Arthrobacter sp.
2.7.1.63 7.5
-
 polyphosphate- and ATP-dependent mannokinase activity, polyphosphate and ATP-dependent glucokinase activity Arthrobacter sp.

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.7.1.63 6 9.5 pH 6.0: about 25% of maximal activity, pH 9.5: about 35% of maximal activity, polyphosphate-dependent and ATP-dependent mannokinase activity, polyphosphate and ATP-dependent glucokinase activity Arthrobacter sp.

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.7 ATP dependent on, can be substituted by polyphosphate, binding site is the same as for polyphosphate binding Arthrobacter sp.