Enzymes
| UniProtKB help_outline | 1 proteins |
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- Name help_outline β-D-fructose 1,6-bisphosphate Identifier CHEBI:32966 (Beilstein: 7104287) help_outline Charge -4 Formula C6H10O12P2 InChIKeyhelp_outline RNBGYGVWRKECFJ-ARQDHWQXSA-J SMILEShelp_outline O[C@H]1[C@H](O)[C@@](O)(COP([O-])([O-])=O)O[C@@H]1COP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 7 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 5,851 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline β-D-fructose 6-phosphate Identifier CHEBI:57634 (Beilstein: 6422468) help_outline Charge -2 Formula C6H11O9P InChIKeyhelp_outline BGWGXPAPYGQALX-ARQDHWQXSA-L SMILEShelp_outline OC[C@@]1(O)O[C@H](COP([O-])([O-])=O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 17 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline phosphate Identifier CHEBI:43474 Charge -2 Formula HO4P InChIKeyhelp_outline NBIIXXVUZAFLBC-UHFFFAOYSA-L SMILEShelp_outline OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 963 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:11064 | RHEA:11065 | RHEA:11066 | RHEA:11067 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Fructose diphosphatase from rabbit liver. I. Purification and properties.
Pontremoli S., Traniello S., Luppis B., Wood W.A.
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Purification and properties of fructose-1, 6-diphosphatase.
MCGILVERY R.W., MOKRASCH L.C.
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MJ0917 in archaeon Methanococcus jannaschii is a novel NADP phosphatase/NAD kinase.
Kawai S., Fukuda C., Mukai T., Murata K.
NAD kinase phosphorylates NAD(+) to form NADP(+). Conversely, NADP phosphatase, which has not yet been identified, dephosphorylates NADP(+) to produce NAD(+). Among the NAD kinase homologs, the primary structure of MJ0917 of hyperthermophilic archaeal Methanococcus jannaschii is unique. MJ0917 pos ... >> More
NAD kinase phosphorylates NAD(+) to form NADP(+). Conversely, NADP phosphatase, which has not yet been identified, dephosphorylates NADP(+) to produce NAD(+). Among the NAD kinase homologs, the primary structure of MJ0917 of hyperthermophilic archaeal Methanococcus jannaschii is unique. MJ0917 possesses an NAD kinase homologous region in its C-terminal half and an inositol-1-phosphatase homologous region in its N-terminal half. In this study, MJ0917 was biochemically shown to possess both NAD kinase and phosphatase activities toward NADP(+), NADPH, and fructose 1,6-bisphosphate, but not toward inositol 1-phosphate. With regard to the phosphatase activity, kinetic values indicated that NADP(+) is the preferred substrate and that MJ0917 would function as a novel NADP phosphatase/NAD kinase showing conflicting dual activities, viz. synthesis and degradation of an essential NADP(+). Furthermore, in vitro analysis of MJ0917 showed that, although MJ0917 could supply NADP(+), it prevented excess accumulation of NADP(+); thus, it has the ability to maintain a high NAD(+)/NADP(+) ratio, whereas 5'-AMP would decrease this ratio. The evolutionary process during which MJ0917 arose is also discussed. << Less
J. Biol. Chem. 280:39200-39207(2005) [PubMed] [EuropePMC]
This publication is cited by 9 other entries.