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IUBMB Comments The enzyme, characterized from the bacteria Actinosynnema mirum and Stigmatella aurantiaca DW4/3-1, produces 2-epi -valiolone, which is believed to function as a precursor in aminocyclitol biosynthesis. It requires a divalent metal ion (Zn2+ 2+ + cf . EC 4.2.3.152 , 2-epi -5-epi -valiolone synthase and EC 4.2.3.154 , demethyl-4-deoxygadusol synthase.
Synonyms aroB , EVS,
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aroB
-
EVS
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D-sedoheptulose 7-phosphate = 2-epi-valiolone + phosphate
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-
-
-
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D-sedoheptulose-7-phosphate phosphate-lyase (cyclizing; 2-epi-valiolone-forming)
The enzyme, characterized from the bacteria Actinosynnema mirum and Stigmatella aurantiaca DW4/3-1, produces 2-epi-valiolone, which is believed to function as a precursor in aminocyclitol biosynthesis. It requires a divalent metal ion (Zn2+ or Co2+) and an NAD+ cofactor, which is transiently reduced during the reaction. cf. EC 4.2.3.152, 2-epi-5-epi-valiolone synthase and EC 4.2.3.154, demethyl-4-deoxygadusol synthase.
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D-sedoheptulose 7-phosphate
2-epi-valiolone + phosphate
D-sedoheptulose 7-phosphate
2-epi-valiolone + phosphate
Substrates: the enzyme produces 2-epi-valiolone, which is believed to function as a precursor in aminocyclitol biosynthesis
?
D-sedoheptulose 7-phosphate
2-epi-valiolone + phosphate
Substrates: -
?
D-sedoheptulose 7-phosphate
2-epi-valiolone + phosphate
Substrates: the enzyme produces 2-epi-valiolone, which is believed to function as a precursor in aminocyclitol biosynthesis
?
D-sedoheptulose 7-phosphate
2-epi-valiolone + phosphate
Substrates: -
?
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D-sedoheptulose 7-phosphate
2-epi-valiolone + phosphate
D-sedoheptulose 7-phosphate
2-epi-valiolone + phosphate
Substrates: the enzyme produces 2-epi-valiolone, which is believed to function as a precursor in aminocyclitol biosynthesis
?
D-sedoheptulose 7-phosphate
2-epi-valiolone + phosphate
Substrates: the enzyme produces 2-epi-valiolone, which is believed to function as a precursor in aminocyclitol biosynthesis
?
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NAD+
the enzyme requires an NAD+ cofactor, which is transiently reduced during the reaction
NAD+
the enzyme requires an NAD+ cofactor, which is transiently reduced during the reaction
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Co2+
the enzyme requires a divalent metal ion (Zn2+ or Co2+)
Co2+
the enzyme requires a divalent metal ion (Zn2+ or Co2+)
Zn2+
the enzyme requires a divalent metal ion (Zn2+ or Co2+)
Zn2+
the enzyme requires a divalent metal ion (Zn2+ or Co2+)
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0.0386 - 0.0599
D-sedoheptulose 7-phosphate
0.0386
D-sedoheptulose 7-phosphate
pH 7.0, 28°C
0.0599
D-sedoheptulose 7-phosphate
pH 7.0, 28°C
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0.033 - 0.062
D-sedoheptulose 7-phosphate
0.033
D-sedoheptulose 7-phosphate
pH 7.0, 28°C
0.062
D-sedoheptulose 7-phosphate
pH 7.0, 28°C
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0.556 - 1.6
D-sedoheptulose 7-phosphate
0.556
D-sedoheptulose 7-phosphate
pH 7.0, 28°C
1.6
D-sedoheptulose 7-phosphate
pH 7.0, 28°C
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7
assay at
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28
assay at
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UniProt
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UniProt
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Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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metabolism
the enzyme produces 2-epi-valiolone, which is believed to function as a precursor in aminocyclitol biosynthesis
metabolism
the enzyme produces 2-epi-valiolone, which is believed to function as a precursor in aminocyclitol biosynthesis
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EVS_ACTMD
Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 / NCIMB 13271 / NRRL B-12336 / IMRU 3971 / 101)
382
0
41009
Swiss-Prot
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EVS_STIAD
Stigmatella aurantiaca (strain DW4/3-1)
406
1
43439
Swiss-Prot
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41009
x * 41009, calculated from sequence
43439
x * 43439, calculated from sequence
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?
x * 41009, calculated from sequence
?
x * 43439, calculated from sequence
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-
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expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
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Asamizu, S.; Xie, P.; Brumsted, C.J.; Flatt, P.M.; Mahmud, T.
Evolutionary divergence of sedoheptulose 7-phosphate cyclases leads to several distinct cyclic products
J. Am. Chem. Soc.
134
12219-12229
2012
Actinosynnema mirum (C6WFL3), Stigmatella aurantiaca (Q08VU0)
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