2.7.1.63: polyphosphate-glucose phosphotransferase
This is an abbreviated version!
For detailed information about polyphosphate-glucose phosphotransferase, go to the full flat file.
Word Map on EC 2.7.1.63
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2.7.1.63
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mycobacterium
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tuberculosis
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6-phosphate
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glucokinases
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shermanii
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propionibacterium
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nonprocessive
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synthesis
- 2.7.1.63
- mycobacterium
- tuberculosis
- 6-phosphate
- glucokinases
- shermanii
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propionibacterium
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nonprocessive
- synthesis
Reaction
Synonyms
All1371, GMK, inorganic polyphosphate/ATP-glucomannokinase, inorganic polyphosphate:D-glucose 6-phosphotransferase, More, PGPTase, phosphotransferase, polyphosphate-glucose, poly P glucokinase, poly(P) glucokinase, poly(P)/ATP-glucomannokinase, PolyP-dependent glucokinase, polyP-GK, polyP-Glk, polyphosphate glucokinase, polyphosphate-D-(+)-glucose-6-phosphotransferase, polyphosphate-dependent glucokinase, polyphosphate-glucose 6-phosphotransferase, polyphosphate/ATP-glucomannokinase, PP-Glk, PPGK, SCO5059
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Reaction
Reaction on EC 2.7.1.63 - polyphosphate-glucose phosphotransferase
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with long chain polyphosphates, the reaction proceeds by a processive type mechanism, with short polyphosphates the mechanism is nonprocessive
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(phosphate)n + D-glucose = (phosphate)n-1 + D-glucose 6-phosphate
in the polyphosphate-dependent reaction the enzyme follows an ordered bi bi sequential mechanism with polyphosphate binding to the enzyme first and glucose 6-phosphate dissociating last. The ATP-dependent glucokinase reaction is consistent with an ordered bi bi sequential mechanism, with ATP binding to the enzyme first and glucose 6-phosphate leaving last
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(phosphate)n + D-glucose = (phosphate)n-1 + D-glucose 6-phosphate
glucose and phosphate substrate binding site structures
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(phosphate)n + D-glucose = (phosphate)n-1 + D-glucose 6-phosphate
glucose and phosphate substrate binding site structures
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