- Maximum activity is only obtained in the presence of alpha-D-glucose
1,6-bisphosphate.
- This bisphosphate is an intermediate in the reaction, being formed by
transfer of a phosphate residue from the enzyme to the substrate,
but the dissociation of bisphosphate from the enzyme complex is much
slower than the overall isomerization.
- Also, more slowly, catalyzes the interconversion of 1-phosphate and
6-phosphate isomers of many other alpha-D-hexoses, and the
interconversion of alpha-D-ribose 1-phosphate and 5-phosphate.
- Formerly EC 2.7.5.1.
|
| UniProtKB/Swiss-Prot |
| P26276, ALGC_PSEAE; | Q88C93, ALGC_PSEPK; | Q88BD4, ALGC_PSESM; |
| P18159, PGCA_BACSU; | Q2FE11, PGCA_STAA3; | Q2FVC1, PGCA_STAA8; |
| Q2YW66, PGCA_STAAB; | Q5HD61, PGCA_STAAC; | Q99RE2, PGCA_STAAM; |
| Q7A3K7, PGCA_STAAN; | Q6GDU9, PGCA_STAAR; | Q6G6I3, PGCA_STAAS; |
| Q8NUV4, PGCA_STAAW; | Q5HLD2, PGCA_STAEQ; | Q8CN38, PGCA_STAES; |
| Q4L9R5, PGCA_STAHJ; | Q49WH7, PGCA_STAS1; | Q08DP0, PGM1_BOVIN; |
| Q23919, PGM1_DICDI; | P36871, PGM1_HUMAN; | Q4R5E4, PGM1_MACFA; |
| Q9D0F9, PGM1_MOUSE; | P47244, PGM1_PARTE; | P00949, PGM1_RABIT; |
| P38652, PGM1_RAT; | P33401, PGM1_YEAST; | Q54UQ2, PGM2_DICDI; |
| Q96G03, PGM2_HUMAN; | Q7TSV4, PGM2_MOUSE; | O02606, PGM2_PARTE; |
| Q5RFI8, PGM2_PONAB; | O74478, PGM2_SCHPO; | P37012, PGM2_YEAST; |
| Q03262, PGM3_YEAST; | O49299, PGMC1_ARATH; | P93804, PGMC1_MAIZE; |
| Q9SGC1, PGMC2_ARATH; | P93805, PGMC2_MAIZE; | Q9SNX2, PGMC_BROIN; |
| P93262, PGMC_MESCR; | Q9SM60, PGMC_PEA; | Q9ZSQ4, PGMC_POPTN; |
| Q9M4G4, PGMC_SOLTU; | Q9SCY0, PGMP_ARATH; | Q9SMM0, PGMP_BRANA; |
| Q9SM59, PGMP_PEA; | Q9M4G5, PGMP_SOLTU; | P38569, PGM_ACEXY; |
| P39671, PGM_AGRTU; | Q4WY53, PGM_ASPFU; | P57749, PGM_ASPOR; |
| Q9VUY9, PGM_DROME; | Q7KHA1, PGM_DROSI; | P36938, PGM_ECOLI; |
| Q9P931, PGM_EMENI; | O18719, PGM_ENTDI; | O15820, PGM_ENTHI; |
| P40390, PGM_NEIGO; | P57002, PGM_NEIMA; | P40391, PGM_NEIMB; |
| O74374, PGM_SCHPO; | B0RVK5, XANA_XANCB; | P0C7J2, XANA_XANCP; |
|
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