3-hexulose-6-phosphate synthase

3-hexulose-6-phosphate synthase (EC 4.1.2.43, D-arabino-3-hexulose 6-phosphate formaldehyde-lyase, 3-hexulosephosphate synthase, 3-hexulose phosphate synthase, HPS) is an enzyme with systematic name D-arabino-hex-3-ulose-6-phosphate formaldehyde-lyase (D-ribulose-5-phosphate-forming).^[1]^[2]^[3]^[4]^[5]^[6]^[7] This enzyme catalyses the following chemical reaction

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

\rightleftharpoons

D-ribulose 5-phosphate + formaldehyde

This enzyme requires Mg²⁺ or Mn²⁺ for maximal activity.

References

↑ Ferenci, T.; Strom, T.; 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.
↑ Kato, N.; Ohashi, H.; Tani, Y.; Ogata, K. (1978). "3-Hexulosephosphate synthase from Methylomonas aminofaciens 77a. Purification, properties and kinetics". Biochim. Biophys. Acta. 523: 236–244. doi:10.1016/0005-2744(78)90026-8. PMID 564713.
↑ Yanase, H.; Ikeyama, K.; Mitsui, R.; Ra, S.; Kita, K.; Sakai, Y.; Kato, N. (1996). "Cloning and sequence analysis of the gene encoding 3-hexulose-6-phosphate synthase from the methylotrophic bacterium, Methylomonas aminofaciens 77a, and its expression in Escherichia coli". FEMS Microbiol. Lett. 135: 201–205. doi:10.1111/j.1574-6968.1996.tb07990.x. PMID 8595859.
↑ Yurimoto, H.; Kato, N.; 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.; 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.; 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.
↑ Kato, N.; Miyamoto, N.; Shimao, M.; Sakazawa, C. (1988). "3-Hexulose phosphate pynthase from a new facultative methylotroph, Mycobacterium gastri MB19". Agric. Biol. Chem. 52: 2659–2661. doi:10.1271/bbb1961.52.2659.

External links

3-hexulose-6-phosphate synthase at the US National Library of Medicine Medical Subject Headings (MeSH)

Carbon-carbon lyases (EC 4.1)

4.1.1: Carboxy-lyases	Acetoacetate decarboxylase Adenosylmethionine decarboxylase Aromatic L-amino acid decarboxylase Glutamate decarboxylase Histidine decarboxylase Lysine decarboxylase Malonyl-CoA decarboxylase Ornithine decarboxylase Oxaloacetate decarboxylase Phosphoenolpyruvate carboxykinase Phosphoenolpyruvate carboxylase Phosphoribosylaminoimidazole carboxylase Pyrophosphomevalonate decarboxylase Pyruvate decarboxylase RuBisCO Uridine monophosphate synthetase/Orotidine 5'-phosphate decarboxylase Uroporphyrinogen III decarboxylase

4.1.2: Aldehyde-lyases	Fructose-bisphosphate aldolase Aldolase A Aldolase B Aldolase C 2-hydroxyphytanoyl-CoA lyase Threonine aldolase

4.1.3: Oxo-acid-lyases	Isocitrate lyase 3-hydroxy-3-methylglutaryl-CoA lyase

4.1.99: Other	Tryptophanase

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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