- Maximum activity is only obtained in the presence of alpha-D-glucose
- 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 220.127.116.11.
- Formerly EC 18.104.22.168.
|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; |