| Entry |
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| Name |
3-hexulose-6-phosphate synthase;
D-arabino-3-hexulose 6-phosphate formaldehyde-lyase;
3-hexulosephosphate synthase;
3-hexulose phosphate synthase;
HPS
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| Class |
Lyases;
Carbon-carbon lyases;
Aldehyde-lyases
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| Sysname |
D-arabino-hex-3-ulose-6-phosphate formaldehyde-lyase (D-ribulose-5-phosphate-forming)
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| Reaction(IUBMB) |
D-arabino-hex-3-ulose 6-phosphate = D-ribulose 5-phosphate + formaldehyde [RN: R05338]
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| Reaction(KEGG) |
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| Substrate |
D-arabino-hex-3-ulose 6-phosphate [CPD: C06019]
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| Product |
D-ribulose 5-phosphate [CPD: C00199];
formaldehyde [CPD: C00067]
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| Comment |
Requires Mg2+ or Mn2+ for maximal activity [1]. The enzyme is specific for D-ribulose 5-phosphate as substrate as ribose 5-phosphate, xylulose 5-phosphate, allulose 6-phosphate and fructose 6-phosphate cannot act as substrate. In addition to formaldehyde, the enzyme can also use glycolaldehyde and methylglyoxal [7]. This enzyme, along with EC 5.3.1.27, 6-phospho-3-hexuloisomerase, plays a key role in the ribulose-monophosphate cycle of formaldehyde fixation, which is present in many microorganisms that are capable of utilizing C1-compounds [1]. The hyperthermophilic and anaerobic archaeon Pyrococcus horikoshii OT3 constitutively produces a bifunctional enzyme that sequentially catalyses the reactions of this enzyme and EC 5.3.1.27, 6-phospho-3-hexuloisomerase [6]. This enzyme is a member of the orotidine 5'-monophosphate decarboxylase (OMPDC) suprafamily [5].
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| History |
EC 4.1.2.43 created 2008
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| Pathway |
| ec01120 | Microbial metabolism in diverse environments |
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| Orthology |
| K08093 | 3-hexulose-6-phosphate synthase |
| K13812 | bifunctional enzyme Fae/Hps |
| K13831 | 3-hexulose-6-phosphate synthase / 6-phospho-3-hexuloisomerase |
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| Genes |
» show all
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| Reference |
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| Authors |
Ferenci T, Strom T, Quayle JR |
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| Title |
Purification and properties of 3-hexulose phosphate synthase and phospho-3-hexuloisomerase from Methylococcus capsulatus. |
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| Journal |
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| Reference |
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| Authors |
Kato N, Ohashi H, Tani Y, Ogata K |
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| Title |
3-Hexulosephosphate synthase from Methylomonas aminofaciens 77a. Purification, properties and kinetics. |
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| Journal |
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| Reference |
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| Authors |
Yanase H, Ikeyama K, Mitsui R, Ra S, Kita K, Sakai Y, Kato N |
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| Title |
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. |
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| Journal |
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| Sequence |
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| Reference |
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| Authors |
Yurimoto H, Kato N, Sakai Y |
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| Title |
Assimilation, dissimilation, and detoxification of formaldehyde, a central metabolic intermediate of methylotrophic metabolism. |
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| Journal |
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| Reference |
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| Authors |
Kato N, Yurimoto H, Thauer RK |
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| Title |
The physiological role of the ribulose monophosphate pathway in bacteria and archaea. |
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| Journal |
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| Reference |
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| Authors |
Orita I, Yurimoto H, Hirai R, Kawarabayasi Y, Sakai Y, Kato N |
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| Title |
The archaeon Pyrococcus horikoshii possesses a bifunctional enzyme for formaldehyde fixation via the ribulose monophosphate pathway. |
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| Journal |
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| Sequence |
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| Reference |
7 |
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| Authors |
Kato, N., Miyamoto, N., Shimao, M. and Sakazawa, C. |
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| Title |
3-Hexulose phosphate pynthase from a new facultative methylotroph, Mycobacterium gastri MB19. |
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| Journal |
Agric Biol Chem 52:2659-2661 (1988) |
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| Other DBs |
| ExplorEnz - The Enzyme Database: | 4.1.2.43 |
| ExPASy - ENZYME nomenclature database: | 4.1.2.43 |
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