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Information on EC 4.2.3.155 - 2-epi-valiolone synthase and Organism(s) Actinosynnema mirum and UniProt Accession C6WFL3

for references in articles please use BRENDA:EC4.2.3.155
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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.3 Acting on phosphates
                4.2.3.155 2-epi-valiolone synthase
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+ 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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This record set is specific for:
Actinosynnema mirum
UNIPROT: C6WFL3
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The taxonomic range for the selected organisms is: Actinosynnema mirum
The enzyme appears in selected viruses and cellular organisms
Synonyms
aroB, EVS, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-sedoheptulose 7-phosphate
2-epi-valiolone + phosphate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-sedoheptulose 7-phosphate
2-epi-valiolone + phosphate
show the reaction diagram
the enzyme produces 2-epi-valiolone, which is believed to function as a precursor in aminocyclitol biosynthesis
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
the enzyme requires an NAD+ cofactor, which is transiently reduced during the reaction
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
the enzyme requires a divalent metal ion (Zn2+ or Co2+)
Zn2+
the enzyme requires a divalent metal ion (Zn2+ or Co2+)
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0599
D-sedoheptulose 7-phosphate
pH 7.0, 28°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.033
D-sedoheptulose 7-phosphate
pH 7.0, 28°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.556
D-sedoheptulose 7-phosphate
pH 7.0, 28°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme produces 2-epi-valiolone, which is believed to function as a precursor in aminocyclitol biosynthesis
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41009
x * 41009, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 41009, calculated from sequence
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team