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D-arabino-3-hexulose 6-phosphate
D-fructose 6-phosphate
D-arabino-3-hexulose 6-phosphate
D-fructose-6-phosphate
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
D-fructose 6-phosphate
D-arabino-3-hexulose 6-phosphate
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-
-
-
r
D-fructose 6-phosphate
D-arabino-hex-3-ulose 6-phosphate
additional information
?
-
D-arabino-3-hexulose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-arabino-3-hexulose 6-phosphate
D-fructose 6-phosphate
-
-
-
?
D-arabino-3-hexulose 6-phosphate
D-fructose 6-phosphate
-
-
-
?
D-arabino-3-hexulose 6-phosphate
D-fructose-6-phosphate
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-
-
-
ir
D-arabino-3-hexulose 6-phosphate
D-fructose-6-phosphate
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-
-
-
ir
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
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-
-
-
?
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
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-
-
-
?
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
?
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
-
-
-
?
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
?
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
?
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
?
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
?
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
?
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
?
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
?
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
?
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
?
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
?
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
?
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
?
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
?
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-fructose 6-phosphate
D-arabino-hex-3-ulose 6-phosphate
-
-
-
-
r
D-fructose 6-phosphate
D-arabino-hex-3-ulose 6-phosphate
-
-
-
-
r
additional information
?
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-
enzyme is specific for substrates D-arabino-3-hexulose 6-phosphate and D-fructose 6-phosphate
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?
additional information
?
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-
no substrate: D-ribulose 5-phosphate, D-xylulose 5-phosphate or D-allulose 6-phosphate
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-
?
additional information
?
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-
bifunctional 3-hexulose-6-phosphate synthase/6-phospho-3-hexuloisomerase is essential for the biosynthesis of ribulose 5-phosphate. The ribulose monophosphate pathway substitutes for the classical pentose phosphate pathway in Thermococcus kodakarensis
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?
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physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
physiological function
-
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
physiological function
3-hexulose-6-phosphate synthase (HPS) and 6-phospho-3-hexulose isomerase (PHI) are encoded by the genes Hps and Phi and the fused gene Hps-Phi (Hpsi2). Both 3-hexulose-6-phosphate synthase plus 6-phospho-3-hexulose isomerase and the fused gene product catalyze formation of fructose 6-phosphate from formaldehyde and ribulose 5-phosphate with activities of 172 and 22 U/mg, respectively. the fusion protein Hpsi2 does not show isomerase activity, but the sequences corresponding to its HPS and PHI regions, when expressed separately, produce active enzymes
physiological function
3-hexulose-6-phosphate synthase (HPS) and 6-phospho-3-hexulose isomerase (PHI) are encoded by the genes Hps and Phi and the fused gene Hps-Phi. Both 3-hexulose-6-phosphate synthase plus 6-phospho-3-hexulose isomerase and the fused gene product catalyze formation of fructose 6-phosphate from formaldehyde and ribulose 5-phosphate with activities of 172 and 22 U/mg, respectively
physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
-
physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
-
physiological function
-
3-hexulose-6-phosphate synthase (HPS) and 6-phospho-3-hexulose isomerase (PHI) are encoded by the genes Hps and Phi and the fused gene Hps-Phi. Both 3-hexulose-6-phosphate synthase plus 6-phospho-3-hexulose isomerase and the fused gene product catalyze formation of fructose 6-phosphate from formaldehyde and ribulose 5-phosphate with activities of 172 and 22 U/mg, respectively
-
physiological function
-
3-hexulose-6-phosphate synthase (HPS) and 6-phospho-3-hexulose isomerase (PHI) are encoded by the genes Hps and Phi and the fused gene Hps-Phi (Hpsi2). Both 3-hexulose-6-phosphate synthase plus 6-phospho-3-hexulose isomerase and the fused gene product catalyze formation of fructose 6-phosphate from formaldehyde and ribulose 5-phosphate with activities of 172 and 22 U/mg, respectively. the fusion protein Hpsi2 does not show isomerase activity, but the sequences corresponding to its HPS and PHI regions, when expressed separately, produce active enzymes
-
physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
-
physiological function
-
6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
-
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Taylor, E.J.; Charnock, S.J.; Colby, J.; Davies, G.J.; Black, G.W.
Cloning, purification and characterization of the 6-phospho-3-hexulose isomerase YckF from Bacillus subtilis
Acta Crystallogr. Sect. D
D57
1138-1140
2001
Bacillus subtilis (P42404)
brenda
Kato, N.; Ohashi, H.; Hori, T.; Tani, Y.; Ogata, K.
Properties of 3-hexulose phosphate synthase and phospho-3-hexuloisomerase of a methanol-utilizing bacterium, 77a
Agric. Biol. Chem.
41
1133-1140
1977
uncultured bacterium, no activity in Hansenula polymorpha, no activity in Kloeckera sp., uncultured bacterium 77a, no activity in Kloeckera sp. 2201, no activity in Hansenula polymorpha DL-1
-
brenda
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
Mycobacterium gastri (Q9LBW5), Mycobacterium gastri MB19 (Q9LBW5), Mycobacterium gastri MB19
brenda
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
Methylococcus capsulatus
brenda
Yanase, H.; Koike, Y.; Matsuzaki, K.; Kita, K.; Sato, Y.; Kato, N.
Production of D-[1-13C]fructose 6-phosphate by a formaldehyde-fixing system in Methylomonas aminofaciens 77a
Biosci. Biotechnol. Biochem.
56
541-542
1992
Methylomonas aminofaciens (Q9S0X3), Methylomonas aminofaciens 77a (Q9S0X3)
brenda
Yasueda, H.; Kawahara, Y.; Sugimoto, S.
Bacillus subtilis yckG and yckF encode two key enzymes of the ribulose monophosphate pathway used by methylotrophs, and yckH is required for their expression
J. Bacteriol.
181
7154-7160
1999
Bacillus subtilis
brenda
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
Pyrococcus horikoshii (O59601), Pyrococcus horikoshii
brenda
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
Thermococcus kodakarensis
brenda
Martinez-Cruz, L.A.; Dreyer, M.K.; Boisvert, D.C.; Yokota, H.; Martinez-Chantar, M.L.; Kim, R.; Kim, S.
Crystal structure of MJ1247 protein from M. jannaschii at 2.0 A resolution infers a molecular function of 3-hexulose-6-phosphate isomerase
Structure
10
195-204
2002
Methanocaldococcus jannaschii (Q58644), Methanocaldococcus jannaschii
brenda
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
Brevibacillus brevis, Bacillus subtilis, Bacillus methanolicus, Methanosarcina sp., Methylococcus capsulatus, Pyrococcus sp., Pyrococcus horikoshii, Thermococcus kodakarensis, Thermococcus sp., Methylobacillus flagellatus KT, Methylomonas aminofaciens, Mycobacterium gastri
brenda
Song, Z.; Orita, I.; Yin, F.; Yurimoto, H.; Kato, N.; Sakai, Y.; Izui, K.; Li, K.; Chen, L.
Overexpression of an HPS/PHI fusion enzyme from Mycobacterium gastri in chloroplasts of geranium enhances its ability to assimilate and phytoremediate formaldehyde
Biotechnol. Lett.
32
1541-1548
2010
Mycobacterium gastri, Mycobacterium gastri MB19
brenda
Witthoff, S.; Schmitz, K.; Niedenfuehr, S.; Noeh, K.; Noack, S.; Bott, M.; Marienhagen, J.
Metabolic engineering of Corynebacterium glutamicum for methanol metabolism
Appl. Environ. Microbiol.
81
2215-2225
2015
Bacillus subtilis (P42404), Bacillus subtilis, Bacillus subtilis 168 (P42404)
brenda
Lessmeier, L.; Pfeifenschneider, J.; Carnicer, M.; Heux, S.; Portais, J.C.; Wendisch, V.F.
Production of carbon-13-labeled cadaverine by engineered Corynebacterium glutamicum using carbon-13-labeled methanol as co-substrate
Appl. Microbiol. Biotechnol.
99
10163-10176
2015
Bacillus subtilis (P42404), Bacillus subtilis 168 (P42404)
brenda
Rozova, O.N.; But, S.Y.; Khmelenina, V.N.; Reshetnikov, A.S.; Mustakhimov, I.I.; Trotsenko, Y.A.
Characterization of two recombinant 3-hexulose-6-phosphate synthases from the halotolerant obligate methanotroph Methylomicrobium alcaliphilum 20Z
Biochemistry (Moscow)
82
176-185
2017
Methylotuvimicrobium alcaliphilum (G4T0K4), Methylotuvimicrobium alcaliphilum (G4T2U5), Methylotuvimicrobium alcaliphilum 20Z (G4T0K4), Methylotuvimicrobium alcaliphilum 20Z (G4T2U5)
brenda