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The enzyme appears in viruses and cellular organisms
Synonyms
mannokinase,
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inorganic polyphosphate/ATP-glucomannokinase
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D-fructose (D-mannose) kinase
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kinase (phosphorylating), mannose-
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kinase, manno- (phosphorylating)
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ATP + D-mannose = ADP + D-mannose 6-phosphate
mechanism, enzyme shows both mannokinase and glucokinase activities
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phospho group transfer
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ATP:D-mannose 6-phosphotransferase
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ATP + D-glucose
ADP + D-glucose 6-phosphate
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ATP + D-mannose
ADP + D-mannose 6-phosphate
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hexametaphosphate + D-mannose
pentaphosphate + D-mannose 6-phosphate
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additional information
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additional information
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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
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additional information
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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
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ATP
dependent on, can be substituted by polyphosphate, binding site is the same as for polyphosphate binding
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Co2+
activates, 86% and 30% activity with polyphosphate and ATP, respectively, compared to Mg2+
Cu2+
activates, 11% activity with polyphosphate compared to Mg2+, no activity with ATP
Fe2+
activates, 15% activity with ATP compared to Mg2+, no activity with polyphosphate
Mg2+
absolutely required, most effective metal ion
Mn2+
activates, 82% and 88% activity with polyphosphate and ATP, respectively, compared to Mg2+
Zn2+
activates, 80% and 19% activity with polyphosphate and ATP, respectively, compared to Mg2+
additional information
activities with different divalent cations in descending order: Mg2+, Mn2+, Co2+, Zn2+, Cu2+, and Fe2+, no activity with Hg2+
additional information
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activities with different divalent cations in descending order: Mg2+, Mn2+, Co2+, Zn2+, Cu2+, and Fe2+, no activity with Hg2+
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Polyphosphate
dependent on, can be substituted by ATP, nonprocessive utilization, binding site is the same as for ATP binding
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0.02
Hexametaphosphate
pH 7.0
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0.064
mannokinase activity with polyphosphate in cell extract
0.077
mannokinase activity with ATP in cell extract
110
purified enzyme, mannokinase activity with ATP
220
purified enzyme, mannokinase activity with polyphosphate
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SwissProt
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SwissProt
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Q7WT42_ARTSK
Arthrobacter sp. (strain KM)
267
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27996
TrEMBL
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40
loss of 50% activity after 5 min
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native enzyme 2200fold and 1375fold determined with polyphosphate and ATP, respectively, to homogeneity
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DNA and amino acid sequence determination and analysis, phylogenetic analysis
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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
Appl. Environ. Microbiol.
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3849-3857
2003
Arthrobacter sp. (Q7WT42), Arthrobacter sp., Arthrobacter sp. KM (Q7WT42)
brenda
2.7.1.7 mannokinase
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The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). 
