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Information on EC 5.1.3.18 - GDP-mannose 3,5-epimerase and Organism(s) Oryza sativa and UniProt Accession A3C4S4

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EC Tree
     5 Isomerases
         5.1 Racemases and epimerases
             5.1.3 Acting on carbohydrates and derivatives
                5.1.3.18 GDP-mannose 3,5-epimerase
IUBMB Comments
The enzyme catalyses the formation of the stable intermediate GDP-beta-L-gulose as well as GDP-beta-L-galactose. The reaction proceeds by C4' oxidation of GDP-alpha-D-mannose followed by epimerization of the C5' position to give GDP-beta-L-4-dehydro-gulose. This intermediate is either reduced to give GDP-beta-L-gulose or the C3' position is epimerized to give GDP-beta-L-4-dehydro-galactose, followed by C4' reduction to yield GDP-beta-L-galactose. Both products serve as intermediates in two different variants of plant L-ascorbate biosynthesis pathways.
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This record set is specific for:
Oryza sativa
UNIPROT: A3C4S4
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Word Map
The taxonomic range for the selected organisms is: Oryza sativa
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
gdp-mannose-3',5'-epimerase, gdp-mannose 3,5-epimerase, gdp-d-mannose 3,5-epimerase, gdp-d-mannose-3',5'-epimerase, gdp-mannose 3',5'-epimerase, gdp-d-mannose 3'',5''-epimerase, gdp-d-mannose 3',5'-epimerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GDP-D-mannose 3'',5''-epimerase
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Epimerase, guanosine diphosphomannose
-
-
-
-
GDP-D-mannose 3,5-epimerase
-
-
-
-
GDP-D-mannose:GDP-L-galactose epimerase
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
GDP-alpha-D-mannose 3,5-epimerase
The enzyme catalyses the formation of the stable intermediate GDP-beta-L-gulose as well as GDP-beta-L-galactose. The reaction proceeds by C4' oxidation of GDP-alpha-D-mannose followed by epimerization of the C5' position to give GDP-beta-L-4-dehydro-gulose. This intermediate is either reduced to give GDP-beta-L-gulose or the C3' position is epimerized to give GDP-beta-L-4-dehydro-galactose, followed by C4' reduction to yield GDP-beta-L-galactose. Both products serve as intermediates in two different variants of plant L-ascorbate biosynthesis pathways.
CAS REGISTRY NUMBER
COMMENTARY hide
72162-82-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GDP-D-mannose
GDP-L-galactose
show the reaction diagram
key enzyme in biosynthesis of vitamin C in plants
-
-
?
GDP-D-mannose
GDP-L-galactose + GDP-L-gulose
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
GDP-D-mannose
GDP-L-galactose
show the reaction diagram
key enzyme in biosynthesis of vitamin C in plants
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
accelerates activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00712 - 0.012
GDP-D-mannose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03 - 0.127
GDP-D-mannose
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8
in absence of NAD+
8 - 8.5
in presence of NAD+
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
without NAD+
25
in presence of NAD+
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression as a fusion protein in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Watanabe, K.; Suzuki, K.; Kitamura, S.
Characterization of a GDP-d-mannose 3'',5''-epimerase from rice
Phytochemistry
67
338-346
2006
Oryza sativa (A3C4S4), Oryza sativa
Manually annotated by BRENDA team