5.4.2.7: phosphopentomutase
This is an abbreviated version!
For detailed information about phosphopentomutase, go to the full flat file.
Word Map on EC 5.4.2.7
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5.4.2.7
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nucleoside
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purine
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5-phosphate
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phosphoglucomutase
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deoxyriboaldolase
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2-deoxyribose
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ribose-5-phosphate
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nucleobase
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phosphorylases
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deoxyribonucleosides
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2'-deoxyribonucleoside
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ribokinase
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1,6-diphosphate
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phosphorolysis
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phosphomutases
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analysis
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biotechnology
- 5.4.2.7
- nucleoside
- purine
- 5-phosphate
- phosphoglucomutase
- deoxyriboaldolase
- 2-deoxyribose
- ribose-5-phosphate
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nucleobase
- phosphorylases
- deoxyribonucleosides
- 2'-deoxyribonucleoside
- ribokinase
- 1,6-diphosphate
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phosphorolysis
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phosphomutases
- analysis
- biotechnology
Reaction
Synonyms
alpha-D-Glucose-1,6-bisphosphate:deoxy-D-ribose-1-phosphate phosphotransferase, alpha-D-ribose1,5-phosphomutase, deoB, Deoxyribomutase, Deoxyribose phosphomutase, EC 2.7.5.6, PGM3, Phosphodeoxyribomutase, Phosphomutase, deoxyribose, phosphopentomutase, Phosphoribomutase, PPM, PPMase
ECTree
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General Information
General Information on EC 5.4.2.7 - phosphopentomutase
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malfunction
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only a deletion mutant of PGM3, not of PGM1 or PGM2, hyperaccumulates ribose-1-phosphate, and shows a strongly increased concentration of ribose 1-phosphate and completely defective recycling of ribose 1-phosphate upon glucose-induced purine nucleoside recycling via the purine salvage pathway
additional information
the active site is located between two independently folded domains. The enzyme engages substrates when the active site nucleophile, Thr85, is phosphorylated
additional information
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the active site is located between two independently folded domains. The enzyme engages substrates when the active site nucleophile, Thr85, is phosphorylated
additional information
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the active site is located between two independently folded domains. The enzyme engages substrates when the active site nucleophile, Thr85, is phosphorylated
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