6-phospho-3-hexuloisomerase

6-phospho-3-hexuloisomerase (EC 5.3.1.27, 3-hexulose-6-phosphate isomerase, phospho-3-hexuloisomerase, PHI, 6-phospho-3-hexulose isomerase, YckF) is an enzyme with system name D-arabino-hex-3-ulose-6-phosphate isomerase.^[1]^[2]^[3]^[4]^[5]^[6] This enzyme catalyses the following chemical reaction

D-arabino-hex-3-ulose 6-phosphate

\rightleftharpoons

D-fructose 6-phosphate

This enzyme plays a key role in the ribulose-monophosphate cycle of formaldehyde fixation.

References

↑ Ferenci, T., Strøm, T. and Quayle, J.R. (1974). "Purification and properties of 3-hexulose phosphate synthase and phospho-3-hexuloisomerase from Methylococcus capsulatus". Biochem. J. 144: 477–486. PMID 4219834.
↑ Yurimoto, H., Kato, N. and Sakai, Y. (2005). "Assimilation, dissimilation, and detoxification of formaldehyde, a central metabolic intermediate of methylotrophic metabolism". Chem. Rec. 5: 367–375. doi:10.1002/tcr.20056. PMID 16278835.
↑ Kato, N., Yurimoto, H. and Thauer, R.K. (2006). "The physiological role of the ribulose monophosphate pathway in bacteria and archaea". Biosci. Biotechnol. Biochem. 70: 10–21. doi:10.1271/bbb.70.10. PMID 16428816.
↑ Orita, I., Yurimoto, H., Hirai, R., Kawarabayasi, Y., Sakai, Y. and Kato, N. (2005). "The archaeon Pyrococcus horikoshii possesses a bifunctional enzyme for formaldehyde fixation via the ribulose monophosphate pathway". J. Bacteriol. 187: 3636–3642. doi:10.1128/jb.187.11.3636-3642.2005. PMID 15901685.
↑ Martinez-Cruz, L.A., Dreyer, M.K., Boisvert, D.C., Yokota, H., Martinez-Chantar, M.L., Kim, R. and Kim, S.H. (2002). "Crystal structure of MJ1247 protein from M. jannaschii at 2.0 Å resolution infers a molecular function of 3-hexulose-6-phosphate isomerase". Structure 10: 195–204. doi:10.1016/s0969-2126(02)00701-3. PMID 11839305.
↑ Taylor, E.J., Charnock, S.J., Colby, J., Davies, G.J. and Black, G.W. (2001). "Cloning, purification and characterization of the 6-phospho-3-hexulose isomerase YckF from Bacillus subtilis". Acta Crystallogr. D Biol. Crystallogr. 57: 1138–1140. doi:10.1107/s090744490100748x. PMID 11468398.

External links

6-phospho-3-hexuloisomerase at the US National Library of Medicine Medical Subject Headings (MeSH)

Isomerases: intramolecular oxidoreductases (EC 5.3)

5.3.1: Aldoses/Ketoses	Triosephosphate isomerase Ribose-5-phosphate isomerase Mannose phosphate isomerase Glucose isomerase

5.3.2: Keto/Enol	Phenylpyruvate tautomerase Oxaloacetate tautomerase

5.3.3: C = C	Steroid D-isomerase Isopentenyl-diphosphate delta isomerase Vinylacetyl-CoA D-isomerase Muconolactone D-isomerase Cholestenol Delta-isomerase (EBP) Methylitaconate D-isomerase Aconitate Delta-isomerase Enoyl CoA isomerase Prostaglandin-A1 Delta-isomerase 5-carboxymethyl-2-hydroxymuconate D-isomerase Isopiperitenone D-isomerase L-dopachrome isomerase Polyenoic fatty acid isomerase

5.3.4: S-S	Protein disulfide-isomerase (PDIA3)

5.3.99: other	Prostaglandin D2 synthase/Prostaglandin-D synthase Prostaglandin E synthase Prostacyclin synthase Thromboxane-A synthase

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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