Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
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MetaCyc Reaction: 3.1.3.9/3.1.3.58

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 3.1.3.9 , 3.1.3.58

Enzymes and Genes:
purple acid phosphatase [multifunctional] Inferred from experiment : PAP26 ( Arabidopsis thaliana col )
glucose-6-phosphatase 2 Inferred from experiment : G6PC2 ( Homo sapiens )
glucose-6-phosphatase 3 Inferred from experiment : G6PC3 ( Homo sapiens )
glucose-6-phosphatase Inferred from experiment : G6PC ( Homo sapiens )
alkaline phosphatase Inferred from experiment : phoA ( Escherichia coli K-12 substr. MG1655 )
phosphosugar phosphatase : yigL ( Escherichia coli K-12 substr. MG1655 )
sugar phosphatase : yfbT ( Escherichia coli K-12 substr. MG1655 )
sugar phosphatase : yidA ( Escherichia coli K-12 substr. MG1655 )
sugar phosphatase : ybiV ( Escherichia coli K-12 substr. MG1655 )

Note that this reaction equation differs from the official Enzyme Commission reaction equation for this EC number, which can be found here .

Reaction Locations: cytosol, periplasmic space (sensu Gram-negative Bacteria)

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: Balanced.

Direct generic reaction:
D-glucopyranose 6-phosphate + H2O → D-glucopyranose + phosphate (3.1.3.9/3.1.3.58)

Enzyme Commission Primary Name for 3.1.3.9: glucose-6-phosphatase

Enzyme Commission Synonyms for 3.1.3.9: glucose 6-phosphate phosphatase

Enzyme Commission Primary Name for 3.1.3.58: sugar-terminal-phosphatase

Enzyme Commission Synonyms for 3.1.3.58: xylitol-5-phosphatase

Standard Gibbs Free Energy (ΔrG in kcal/mol): 7.2170105 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary for 3.1.3.9:
Wide distribution in animal tissues. Also catalyses potent transphosphorylations from carbamoyl phosphate, hexose phosphates, diphosphate, phosphoenolpyruvate and nucleoside di- and triphosphates, to D-glucose, D-mannose, 3-methyl-D-glucose or 2-deoxy-D-glucose [cf. EC 2.7.1.62 (phosphoramidate—hexose phosphotransferase}, EC 2.7.1.79 (diphosphate—glycerol phosphotransferase) and EC 3.9.1.1 (phosphoamidase)].

Enzyme Commission Summary for 3.1.3.58:
Acts on sugars and polyols phosphorylated on the terminal carbon, with a preference for sugars with a D-erythro-configuration, e.g. good substrates are glucose 6-phosphate, mannose 6-phosphate, 6-phosphogluconate, erythrose 4-phosphate and xylitol 5-phosphate.

Citations: [Anchors75, Colilla75, Nordlie74, London85]

Gene-Reaction Schematic: ?

Instance reaction of [D-glucopyranose 6-phosphate + H2O → D-glucopyranose + phosphate] (3.1.3.9/3.1.3.58):
i1: β-D-glucose 6-phosphate + H2O → β-D-glucose + phosphate (3.1.3.9/3.1.3.58)

Relationship Links: BRENDA:EC:3.1.3.9 , BRENDA:EC:3.1.3.58 , ENZYME:EC:3.1.3.9 , ENZYME:EC:3.1.3.58 , IUBMB-ExplorEnz:EC:3.1.3.9 , IUBMB-ExplorEnz:EC:3.1.3.58 , UniProt:RELATED-TO:P35575 , UniProt:RELATED-TO:P35576 , UniProt:RELATED-TO:P43428

Credits:
Revised 06-Apr-2011 by Caspi R , SRI International


References

Anchors75: Anchors JM, Karnovsky ML (1975). "Purification of cerebral glucose-6-phosphatase. An enzyme involved in sleep." J Biol Chem 250(16);6408-16. PMID: 169241

Colilla75: Colilla W, Jorgenson RA, Nordlie RC (1975). "Mammalian carbamyl phosphate : glucose phosphotransferase and glucose-6-phosphate phosphohydrolase: extended tissue distribution." Biochim Biophys Acta 377(1);117-25. PMID: 164220

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

London85: London J, Hausman SZ, Thompson J (1985). "Characterization of a membrane-regulated sugar phosphate phosphohydrolase from Lactobacillus casei." J Bacteriol 163(3);951-6. PMID: 2993253

Nordlie74: Nordlie RC (1974). "Metabolic regulation by multifunctional glucose-6-phosphatase." Curr Top Cell Regul 8(0);33-117. PMID: 4370737


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sun Dec 21, 2014, BIOCYC14B.