Enzymes
| UniProtKB help_outline | 276 proteins |
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- 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 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline N-phosphocreatine Identifier CHEBI:58092 Charge -2 Formula C4H8N3O5P InChIKeyhelp_outline DRBBFCLWYRJSJZ-UHFFFAOYSA-L SMILEShelp_outline CN(CC([O-])=O)C(=[NH2+])NP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline creatine Identifier CHEBI:57947 Charge 0 Formula C4H9N3O2 InChIKeyhelp_outline CVSVTCORWBXHQV-UHFFFAOYSA-N SMILEShelp_outline CN(CC([O-])=O)C(N)=[NH2+] 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 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 983 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:12977 | RHEA:12978 | RHEA:12979 | RHEA:12980 | |
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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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Substrate specificity of phosphoprotein phosphatase from spleen.
SUNDARARAJAN T.A., SARMA P.S.
Biochem J 71:537-544(1959) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Some properties of beef spleen phosphoamidase.
SINGER M.F., FRUTON J.S.
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Phosphoramidates. V. Probable identity of rat liver microsomal glucose 6-phosphatase, phosphoramidase, and phosphoramidate-hexose phosphotransferase.
Parvin R., Smith R.A.
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Mitochondrial TNAP controls thermogenesis by hydrolysis of phosphocreatine.
Sun Y., Rahbani J.F., Jedrychowski M.P., Riley C.L., Vidoni S., Bogoslavski D., Hu B., Dumesic P.A., Zeng X., Wang A.B., Knudsen N.H., Kim C.R., Marasciullo A., Millan J.L., Chouchani E.T., Kazak L., Spiegelman B.M.
Adaptive thermogenesis has attracted much attention because of its ability to increase systemic energy expenditure and to counter obesity and diabetes<sup>1-3</sup>. Recent data have indicated that thermogenic fat cells use creatine to stimulate futile substrate cycling, dissipating chemical energ ... >> More
Adaptive thermogenesis has attracted much attention because of its ability to increase systemic energy expenditure and to counter obesity and diabetes<sup>1-3</sup>. Recent data have indicated that thermogenic fat cells use creatine to stimulate futile substrate cycling, dissipating chemical energy as heat<sup>4,5</sup>. This model was based on the super-stoichiometric relationship between the amount of creatine added to mitochondria and the quantity of oxygen consumed. Here we provide direct evidence for the molecular basis of this futile creatine cycling activity in mice. Thermogenic fat cells have robust phosphocreatine phosphatase activity, which is attributed to tissue-nonspecific alkaline phosphatase (TNAP). TNAP hydrolyses phosphocreatine to initiate a futile cycle of creatine dephosphorylation and phosphorylation. Unlike in other cells, TNAP in thermogenic fat cells is localized to the mitochondria, where futile creatine cycling occurs. TNAP expression is powerfully induced when mice are exposed to cold conditions, and its inhibition in isolated mitochondria leads to a loss of futile creatine cycling. In addition, genetic ablation of TNAP in adipocytes reduces whole-body energy expenditure and leads to rapid-onset obesity in mice, with no change in movement or feeding behaviour. These data illustrate the critical role of TNAP as a phosphocreatine phosphatase in the futile creatine cycle. << Less