Information on EC 5.1.3.18 - GDP-mannose 3,5-epimerase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
5.1.3.18
-
RECOMMENDED NAME
GeneOntology No.
GDP-mannose 3,5-epimerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
GDP-alpha-D-mannose = GDP-beta-L-galactose
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
epimerization
-
-
H-transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
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-
Ascorbate and aldarate metabolism
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Biosynthesis of secondary metabolites
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extended VTC2 cycle
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GDP-L-galactose biosynthesis
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L-ascorbate biosynthesis I (L-galactose pathway)
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Metabolic pathways
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VTC2 cycle
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ascorbate metabolism
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SYSTEMATIC NAME
IUBMB Comments
GDP-mannose 3,5-epimerase
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CAS REGISTRY NUMBER
COMMENTARY hide
72162-82-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cv. qinmei, gene GME
UniProt
Manually annotated by BRENDA team
gene GME
UniProt
Manually annotated by BRENDA team
var. Newhall and Dream
-
-
Manually annotated by BRENDA team
var. Egan No.2 and Guoqing No.1
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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silencing of the two GME genes in tomato leaves results in approximately a 60% decrease in terminal L-galactose content in the side chain A of rhamnogalacturonan II as well as in a lower capacity of rhamnogalacturonan II to perform in muro cross-linking
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GDP-alpha-D-mannose
GDP-beta-L-galactose
show the reaction diagram
GDP-alpha-D-mannose
GDP-beta-L-galactose + GDP-beta-L-gulose
show the reaction diagram
-
-
-
-
?
GDP-D-mannose
GDP-L-galactose
show the reaction diagram
GDP-D-mannose
GDP-L-galactose + GDP-L-gulose
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
GDP-alpha-D-mannose
GDP-beta-L-galactose
show the reaction diagram
-
GDP-D-mannose undergoes double epimerization catalyzed by GDP-D-mannose-3',5'-epimerase to form GDP-L-galactose
-
-
?
GDP-D-mannose
GDP-L-galactose
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
-
stimulates
NADP+
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stimulates
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
GDP-D-glucose
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potent competitive inhibitor
GDP-L-fucose
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complex type of inhibition, IC50: 0.07 mM
L-ascorbic acid
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1 mM, 15% inhibition
L-galactono-1,4-lactone
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1 mM, 14% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
accelerates activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0045 - 0.096
GDP-D-mannose
0.097
GDP-L-galactose
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-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007 - 0.127
GDP-D-mannose
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07
GDP-L-fucose
Arabidopsis thaliana
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complex type of inhibition, IC50: 0.07 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8
in absence of NAD+
8 - 8.5
in presence of NAD+
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
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pH 7: 83% of maximal activity, pH 9: 88% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
without NAD+
25
in presence of NAD+
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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secreting
Manually annotated by BRENDA team
; isoform GME2 transcript content is high in flowers
Manually annotated by BRENDA team
quantitative enzyme expression analysis during fruit development and ripening in fruit pulp
Manually annotated by BRENDA team
; isoform GME2 transcript content is low in leaves
Manually annotated by BRENDA team
; isoform GME2 transcript content is moderate in leaves
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42460
isoform GME1, calculated from amino acid sequence
42550
isoform GME2, calculated from amino acid sequence
42759
2 * 42759, calculation from nucleotide sequence
84000
gel filtration
100000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 42759, calculation from nucleotide sequence
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, structures of complexes of the enzyme with GDP-alpha-D-mannose, GDP-beta-L-galactose and a mixture of GDP-beta-L-gulose. Structure of native wild-type enzyme in complex with GDP-D-mannose, native GME K178R, SeMet GME K178E, native GME Y174F in complex with GDP-L-galactose and native GME K217A in complex with GDP-D-mannose
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression as a fusion protein in Escherichia coli
expression in Escherichia coli
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gene GME, promoter sequence determination and comparison, and of cis-acting elements involved in stress-responsive expression, Agrobacterium tumefaciens-mediated transient expression in Nicotiana tabacum cv. NC89
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme downregulated by gibberellin
the enzyme is downregulated by gibberellin
the enzyme is upregulated in the leaves by salicylic acid, wounding, cold, and heat
the enzyme is upregulated in the leaves by salicylic acid, wounding, cold, and heatt
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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construction of transgenic tomato lines RNAi-silenced for GME, RNAi silencing of GME in tomato effectively reduces ascorbate content in the plant, leading to ROS accumulation, leaf bleaching and developmental defects. Transgenic plants display strong alterations in cell-wall composition, with a considerable impact on plant and fruit mechanical properties, GME-silenced lines have increased fragility, phenotype, overview