- 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.
- Cf. EC 5.4.2.5.
- Formerly EC 2.7.5.1.
|
| UniProtKB/Swiss-Prot |
| Q02E40, ALGC_PSEAB; | 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; | P37012, PGM2_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; |
| Q68BJ6, PGMMM_THEKO; | Q9SCY0, PGMP_ARATH; | Q9SMM0, PGMP_BRANA; |
| Q9SM59, PGMP_PEA; | Q9M4G5, PGMP_SOLTU; | Q4WY53, PGM_ASPFU; |
| P57749, PGM_ASPOR; | Q9VUY9, PGM_DROME; | P36938, PGM_ECOLI; |
| Q9P931, PGM_EMENI; | O18719, PGM_ENTDI; | O15820, PGM_ENTHI; |
| P38569, PGM_KOMXY; | P40390, PGM_NEIGO; | P57002, PGM_NEIMA; |
| P40391, PGM_NEIMB; | P39671, PGM_RHIRD; | O74374, PGM_SCHPO; |
| B0RVK5, XANA_XANCB; | P0C7J2, XANA_XANCP; |
|