5.4.2.8: phosphomannomutase
This is an abbreviated version!
For detailed information about phosphomannomutase, go to the full flat file.
Word Map on EC 5.4.2.8
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5.4.2.8
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carbohydrate-deficient
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transferrin
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gdp-mannose
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multisystemic
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cdg-ia
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team
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mannose-1-phosphate
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pectoralis
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phosphoglucomutase
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doctors
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obstetric
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hypoglycosylation
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nipple
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lipid-linked
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psoas
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premammillary
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strabismus
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paromomycin
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meniscectomy
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medicine
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food industry
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biotechnology
- 5.4.2.8
-
carbohydrate-deficient
- transferrin
- gdp-mannose
-
multisystemic
-
cdg-ia
-
team
- mannose-1-phosphate
-
pectoralis
- phosphoglucomutase
-
doctors
-
obstetric
-
hypoglycosylation
-
nipple
-
lipid-linked
-
psoas
-
premammillary
-
strabismus
- paromomycin
-
meniscectomy
- medicine
- food industry
- biotechnology
Reaction
Synonyms
alpha-D-phosphohexomutase, alpha-phosphomannomutase1, EC 2.7.5.7, IMP-sensitive glucose-1,6-bisphosphatase, ManB, ORF17, PGM/PMM, PGM2, PgmG, phosphoglucomutase/phosphomannomutase, Phosphohexomutase, phosphomannomutase, phosphomannomutase 1, phosphomannomutase 2, phosphomannomutase/phosphoglucomutase, phosphomannomutase2, Phosphomannose mutase, Phosphomutase, mannose, PMM, PMM-1, PMM-2, PMM-A1, PMM-A2, PMM-B1, PMM-B2, PMM-D1, PMM-D2, PMM/PGM, PMM1, PMM2, PMMH-22, SP-2, SSO0207
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Posttranslational Modification
Posttranslational Modification on EC 5.4.2.8 - phosphomannomutase
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phosphoprotein
active form of PMM/PGM is phosphorylated at Ser108
phosphoprotein
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mutation of serine 108 where phosphorylation occurs results in phosphorylation of a different residue, so that activity is reduced only 20fold from that of wild-type
phosphoprotein
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phosphorylation of conserved catalytic active site residue Ser108 has broad effects on residues in multiple domains. Dephosphorylation of the enzyme may play two critical functional roles: a direct role in the chemical step of phosphoryl transfer and secondly through propagation of structural flexibility. Dephosphorylation has minimal effects on crystal structure of the enzyme
phosphoprotein
the enzyme requires conserved phosphoserine 108 for activity