Nomenclature
EC number
4.1.2.43
Systematic name
d-arabino-hex-3-ulose-6-phosphate formaldehyde-lyase (D-ribulose-5-phosphate-forming)
Recommended name
3-hexulose-6-phosphate synthase
Synonyms
3-hexulose phosphate synthase <8,15,23> [2,7,9]
3-hexulose-6-phosphate formaldehyde lyase <24> [8]
3-hexulose-6-phosphate synthase <1,2,3,5,7,8,10,11,12,14,15,17,19,20,21,22,23,24,25,26,27,28> (<12> 3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase activities are expressed constitutively in archea [13]) [1,3,4,8,13,14,22]
3-hexulose-phosphate synthase <15> [18]
3-hexulosephosphate synthase <4,6,8,9,13,15,16,22> [5,6,12,20,21]
d-arabino-3-hexulose 6-phosphate formaldehyde lyase <8,22> [2,12]
d-arabino-3-hexulose 6-phosphate formaldehyde-lyase
Fae-Hps <1> (<1> protein with hexulose-6-phosphate synthase and formaldehyde activating enzyme activities [10]) [10]
HPS <1,2,3,4,5,6,7,8,9,10,11,12,13,14,15,16,17,18,19,20,21,22,23,24,25,26,27,28> (<1,5,7,8,15,19,22,23> 3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase activities are expressed constitutively in archea [13]) [1,2,3,5,6,7,8,13,16,17,18,19,20,21,22]
HPS-PHI <12> (<12> bifunctional enzyme with 3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase activities [3]) [3]
HPS-aldolase <15> [9]
HPS/PHI <17> (<17> bifunctional fusion enzyme [4])
[4] hexose phosphate synthase <8> [11]
hexulose-6-phosphate synthase <1> [10]
CAS registry number
55576-36-8
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Orita, I.; Sakamoto, N.; Kato, N.; Yurimoto, H.; Sakai, Y.: Bifunctional enzyme fusion of 3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase. Appl. Microbiol. Biotechnol., 76, 439-445 (2007)
Ferenci, T.; Stroem, T.; Quayle, J.R.: Purification and properties of 3-hexulose phosphate synthase and phospho-3-hexuloisomerase from Methylococcus capsulatus. Biochem. J., 144, 477-486 (1974)
Orita, I.; Yurimoto, H.; Hirai, R.; Kawarabayasi, Y.; Sakai, Y.; Kato, N.: The archaeon Pyrococcus horikoshii possesses a bifunctional enzyme for formaldehyde fixation via the ribulose monophosphate pathway. J. Bacteriol., 187, 3636-3642 (2005)
Orita, I.; Sato, T.; Yurimoto, H.; Kato, N.; Atomi, H.; Imanaka, T.; Sakai, Y.: The ribulose monophosphate pathway substitutes for the missing pentose phosphate pathway in the archaeon Thermococcus kodakaraensis. J. Bacteriol., 188, 4698-4704 (2006)
Mueller, R.; Babel, W.: Multiplicity of 3-hexulosephosphate synthase from bacterium MB 58. 1. Product-induced transition in velocity. Acta Biol. Med. Ger., 40, 123-135 (1981)
Mueller, R.; Babel, W.: Multiplicity of 3-hexulosephosphate synthase from bacterium MB 58. 2. Generation of complex kinetic characteristics. Acta Biol. Med. Ger., 40, 137-146 (1981)
Kato, N.; Miyamoto, N.; Shimao, M.; Sakazawa, C.: 3-Hexulose phosphate synthase from a new facultative methylotroph, Mycobacterium gastri MB19. Agric. Biol. Chem., 52, 2659-2661 (1988)
Taylor, E.J.; Smith, N.L.; Colby, J.; Charnock, S.J.; Black, G.W.: The gene encoding the ribulose monophosphate pathway enzyme, 3-hexulose-6-phosphate synthase, from Aminomonas aminovorus C2A1 is adjacent to coding sequences that exhibit similarity to histidine biosynthesis enzymes. Antonie van Leeuwenhoek, 86, 167-172 (2004)
Beisswenger, R.; Kula, M.R.: Catalytic properties and substrate specificity of 3-hexulose phosphate synthase from Methylomonas M15. Appl. Microbiol. Biotechnol., 34, 604-607 (1991)
Goenrich, M.; Thauer, R.K.; Yurimoto, H.; Kato, N.: Formaldehyde activating enzyme (Fae) and hexulose-6-phosphate synthase (Hps) in Methanosarcina barkeri: a possible function in ribose-5-phosphate biosynthesis. Arch. Microbiol., 184, 41-48 (2005)
Kemp, M.B.: Hexose phosphate synthase from Methylcoccus capsulatus makes d-arabino-3-hexulose phosphate. Biochem. J., 139, 129-134 (1974)
Kato, N.; Ohashi, H.; Tani, Y.; Ogata, K.: 3-Hexulosephosphate synthase from Methylomonas aminofaciens 77a. Purification, properties and kinetics. Biochim. Biophys. Acta, 523, 236-244 (1978)
Kato, N.; Yurimoto, H.; Thauer, R.K.: The physiological role of the ribulose monophosphate pathway in bacteria and archaea. Biosci. Biotechnol. Biochem., 70, 10-21 (2006)
Arfman, N.; Bystrykh, L.V.; Govorukhina, N.I.; Dijkhuizen, L.: 3-Hexulose-6-phosphate synthase from thermotolerant methylotroph Bacillus C1. Methods Enzymol., 188, 391-397 (1990)
Kato, N.: 3-Hexulose-6-phosphate synthase from Mycobacterium gastri MB19. Methods Enzymol., 188, 397-401 (1990)
Mueller, R.H.; Babel, W.: 3-Hexulose-6-phosphate synthase from Acetobacter methanolicus MB58. Methods Enzymol., 188, 401-405 (1990)
Quayle, J.R.: 3-Hexulose-6-phosphate synthase from Methylomonas (Methylococcus) capsulatus. Methods Enzymol., 90, 314-319 (1982)
Sahm, H.; Schuette, H.; Kula, M.R.: 3-Hexulose-phosphate synthase from Methylomonas M15. Methods Enzymol., 90, 319-323 (1982)
Yurimoto, H.; Hirai, R.; Matsuno, N.; Yasueda, H.; Kato, N.; Sakai, Y.: HxlR, a member of the DUF24 protein family, is a DNA-binding protein that acts as a positive regulator of the formaldehyde-inducible hxlAB operon in Bacillus subtilis. Mol. Microbiol., 57, 511-519 (2005)
Mueller, R.; Sokolov, A.P.: Kinetic properties of the purified 3-hexulosephosphate synthase from Pseudomonas oleovorans. Z. Allg. Mikrobiol., 19, 261-267 (1979)
Mueller, R.; Babel, W.: A critical analysis of kinetic data of 3-hexulosephosphate synthases. Michaelis-Menten or complex characteristics. Z. Allg. Mikrobiol., 20, 325-333 (1980)
Yurimoto, H.; Kato, N.; Sakai, Y.: Genomic organization and biochemistry of the ribulose monophosphate pathway and its application in biotechnology. Appl. Microbiol. Biotechnol., 84, 407-416 (2009)
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2013 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Schomburg, D., Schomburg, I. (2013). 3-hexulose-6-phosphate synthase 4.1.2.43. In: Schomburg, D., Schomburg, I. (eds) Class 3.4–6 Hydrolases, Lyases, Isomerases, Ligases. Springer Handbook of Enzymes, vol 10. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-36260-6_33
Download citation
DOI: https://doi.org/10.1007/978-3-642-36260-6_33
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-36259-0
Online ISBN: 978-3-642-36260-6
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)