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Information on EC 5.1.3.18 - GDP-mannose 3,5-epimerase
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5.1.3.18 GDP-mannose 3,5-epimeraseIUBMB 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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Word Map
- 5.1.3.18
- ascorbate
- asa
-
l-ascorbic
- tomato
- phosphorylase
-
pyrophosphorylase
-
l-galactose-1-phosphate
- l-galactono-1,4-lactone
- lycopersicum
- dehydroascorbate
- gpp
-
epimerization
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Epimerase, guanosine diphosphomannose
-
-
-
-
GDP-D-mannose 3',5'-epimerase
GDP-D-mannose 3,5-epimerase
GDP-D-mannose-3',5'-epimerase
GDP-D-mannose:GDP-L-galactose epimerase
-
-
-
-
GME
GDP-D-mannose 3,5-epimerase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GDP-alpha-D-mannose = GDP-beta-L-gulose
(2)
-
-
-
GDP-alpha-D-mannose = GDP-beta-L-galactose
epimerization proceeds via ene-diol intermediates
-
GDP-alpha-D-mannose = GDP-beta-L-galactose
epimerization does not involve the formation of a deoxysugar
-
-
-
GDP-alpha-D-mannose = GDP-beta-L-galactose
beta-L-galactopyranosyl phosphate is an intermediate
-
GDP-alpha-D-mannose = GDP-beta-L-galactose
(1)
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
epimerization
-
-
H-transfer
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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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.
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CAS REGISTRY NUMBER
COMMENTARY
72162-82-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GDP-alpha-D-mannose
GDP-beta-L-galactose
-
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
-
the reaction mixture contains at equilibrium GDP-D-mannose, GDP-L-galactose and GDP-L-gulose in a ratio of 1:0.4:0.2
-
r
GDP-D-mannose
GDP-L-galactose
-
the enzyme catalyzes a reversible epimerization that precedes the committed step in the biosynthesis of vitamin C, resulting in the hydrolysis of the highly energetic glycosyl-diphosphoryl linkage. The plant enzyme undergoes a complex regulation and could control the carbonflux into the vitamin C pathway in response to the redox state of thecell, stress conditions, and GDP-sugar demand for the cell wall glycoprotein biosynthesis
-
r
GDP-D-mannose
GDP-L-galactose
key enzyme in biosynthesis of vitamin C in plants
-
-
?
additional information
?
-
key enzyme of the plant vitamin C pathway
-
?
additional information
?
-
-
key enzyme of the plant vitamin C pathway
-
?
additional information
?
-
-
methyl jasmonate stimulates the de novo biosynthesis of vitamin C in plant cell suspensions. This stimulation coincides with enhanced transcription of GDP-mannose 3'',5''-epimerase
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GDP-alpha-D-mannose
GDP-beta-L-galactose
-
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
-
the enzyme catalyzes a reversible epimerization that precedes the committed step in the biosynthesis of vitamin C, resulting in the hydrolysis of the highly energetic glycosyl-diphosphoryl linkage. The plant enzyme undergoes a complex regulation and could control the carbonflux into the vitamin C pathway in response to the redox state of thecell, stress conditions, and GDP-sugar demand for the cell wall glycoprotein biosynthesis
-
r
GDP-D-mannose
GDP-L-galactose
key enzyme in biosynthesis of vitamin C in plants
-
-
?
additional information
?
-
key enzyme of the plant vitamin C pathway
-
?
additional information
?
-
-
key enzyme of the plant vitamin C pathway
-
?
additional information
?
-
-
methyl jasmonate stimulates the de novo biosynthesis of vitamin C in plant cell suspensions. This stimulation coincides with enhanced transcription of GDP-mannose 3'',5''-epimerase
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.031
GDP-D-mannose
-
recombinant enzyme with N-terminal glutathione-S-transferase tag
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
GDP-D-mannose
-
recombinant enzyme with N-terminal glutathione-S-transferase tag
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
simple and accurate method to measure enzyme activity in plant tissues. The method can be used also to determine the dehydro-L-ascorbate/ascorbic acid ratio as well as the capacity of cells to regenerate ascorbic acid in its reduced form under different physiological conditions
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9
-
pH 7: 83% of maximal activity, pH 9: 88% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
quantitative enzyme expression analysis during fruit development and ripening in fruit pulp
brenda
isoform GME2 transcript content is high in flowers
brenda
-
quantitative enzyme expression analysis during fruit development and ripening in fruit pulp
brenda
quantitative enzyme expression analysis during fruit development and ripening in fruit pulp
brenda
isoform GME2 transcript content is low in differential stages of fruits
brenda
-
expression is low at pre-ripening stage and increases thereafter
brenda
isoform GME2 transcript content is high in leaves
brenda
isoform GME2 transcript content is low in leaves
brenda
isoform GME2 transcript content is moderate in leaves
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
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
metabolism
-
GME is a central enzyme of the major ascorbate biosynthesis pathway in higher plants, it play a key role in the regulation of ascorbate biosynthesis in plants, adjusting the balance between ascorbate and cell-wall monosaccharide biosynthesis. GDP-D-mannose synthesis is the initial step in the pathway of ascorbate biosynthesis, and GDP-D-mannose is also a known precursor for the synthesis of D-mannose, L-fucose and L-galactose, and therefore for hemicelluloses such s the (galacto)glucomannans and for the pectin rhamnogalacturonan II
metabolism
GDP-D-mannose 3',5'-epimerase catalyses a committed step in ascorbic acid biosynthesis
metabolism
GDP-D-mannose 3',5'-epimerase catalyses a committed step in ascorbic acid biosynthesis
physiological function
transgenic plants over-expressing isoform GME1 exhibit a significant increase in total ascorbic acid in leaves and red fruits compared with wild type plants and improved tolerance to methyl viologen, cold, and salt stresses
physiological function
transgenic plants over-expressing isoform GME2 exhibit a significant increase in total ascorbic acid in leaves and red fruits compared with wild type plants and improved tolerance to methyl viologen, cold, and salt stresses
physiological function
GDP-D-mannose 3',5'-epimerase catalyses a committed step in ascorbic acid biosynthesis, ascorbic acid plays important roles in antioxidative defenses against environmental stresses in higher plants
physiological function
GDP-D-mannose 3',5'-epimerase catalyses a committed step in ascorbic acid biosynthesis, ascorbic acid plays important roles in antioxidative defenses against environmental stresses in higher plants
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GME_ARATH
377
0
42758
Swiss-Prot
other Location (Reliability: 2)
GME1_ORYSI
378
0
42808
Swiss-Prot
other Location (Reliability: 2)
GME1_ORYSJ
378
0
42778
Swiss-Prot
other Location (Reliability: 2)
GME2_ORYSJ
371
0
42132
Swiss-Prot
other Location (Reliability: 2)
A0A445LGN0_GLYSO
331
0
37613
TrEMBL
other Location (Reliability: 2)
A1Y2Z3_VITVI
106
0
11967
TrEMBL
other Location (Reliability: 2)
A0A445F931_GLYSO
376
0
42481
TrEMBL
other Location (Reliability: 2)
A0A0B2SLQ7_GLYSO
116
1
12948
TrEMBL
other Location (Reliability: 4)
A0A2N9N918_9BACT
334
0
37904
TrEMBL
-
C6K2K9_SOLLC
376
0
42456
TrEMBL
other Location (Reliability: 2)
F8L5C9_SIMNZ
Simkania negevensis (strain ATCC VR-1471 / Z)
332
0
37690
TrEMBL
-
M2XU23_GALSU
356
0
40564
TrEMBL
other Location (Reliability: 3)
A0A7C9DWT6_OPUST
377
0
42767
TrEMBL
other Location (Reliability: 2)
A0A445INC7_GLYSO
376
0
42580
TrEMBL
other Location (Reliability: 2)
A0A0D2MXR7_9CHLO
399
0
44958
TrEMBL
other Location (Reliability: 3)
C6K2L1_SOLPN
376
0
42490
TrEMBL
other Location (Reliability: 2)
B6ZL92_PRUPE
376
0
42584
TrEMBL
other Location (Reliability: 2)
A0A072VLZ2_MEDTR
380
0
42820
TrEMBL
other Location (Reliability: 2)
B9SZ78_RICCO
376
0
42507
TrEMBL
other Location (Reliability: 2)
A0A5B7B928_DAVIN
104
0
11567
TrEMBL
other Location (Reliability: 3)
A0A1D8QQD2_GRALE
397
0
44254
TrEMBL
other Location (Reliability: 3)
A0A445FL27_GLYSO
376
0
42568
TrEMBL
other Location (Reliability: 3)
G8P152_GRAMM
Granulicella mallensis (strain ATCC BAA-1857 / DSM 23137 / MP5ACTX8)
330
0
36475
TrEMBL
-
A0A2G9GYJ7_9LAMI
376
0
42410
TrEMBL
other Location (Reliability: 2)
A0A2G9G011_9LAMI
376
0
42511
TrEMBL
other Location (Reliability: 2)
I0K0X9_METFB
Methylacidiphilum fumariolicum (strain SolV)
325
0
36976
TrEMBL
-
A0A0D6EW04_9PROT
325
0
36737
TrEMBL
-
E6Q515_9ZZZZ
442
1
48958
TrEMBL
Mitochondrion (Reliability: 3)
A0A7U7B2V8_9PROT
335
1
37394
TrEMBL
-
A0A5B7C9W8_DAVIN
366
0
41474
TrEMBL
other Location (Reliability: 2)
A0A0B2RAA1_GLYSO
356
0
40058
TrEMBL
other Location (Reliability: 2)
A0A1Z5JTK3_FISSO
362
0
40432
TrEMBL
other Location (Reliability: 1)
A0A2P6QPY3_ROSCH
372
0
42115
TrEMBL
other Location (Reliability: 4)
C7CKH0_METED
Methylorubrum extorquens (strain DSM 6343 / CIP 106787 / DM4)
315
0
35125
TrEMBL
-
A0A7C9E1G6_OPUST
109
0
12042
TrEMBL
other Location (Reliability: 3)
A0A5B6ZH56_DAVIN
376
0
42265
TrEMBL
other Location (Reliability: 3)
A0A2P6R5Y3_ROSCH
376
0
42357
TrEMBL
other Location (Reliability: 2)
A0A5B7CAT3_DAVIN
376
0
42459
TrEMBL
other Location (Reliability: 2)
A0A445FL71_GLYSO
280
0
32114
TrEMBL
other Location (Reliability: 3)
A0A5E6MFU3_9BACT
328
0
36789
TrEMBL
-
C5AQ90_METEA
Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1)
315
0
35125
TrEMBL
-
A0A0B2RGZ9_GLYSO
99
0
11358
TrEMBL
other Location (Reliability: 2)
A0A445F8Y3_GLYSO
329
0
37259
TrEMBL
other Location (Reliability: 2)
A0A2I0BAW9_9ASPA
378
0
42701
TrEMBL
other Location (Reliability: 3)
A0A2U3KM14_9BACT
341
1
38734
TrEMBL
-
A0A445FL83_GLYSO
330
0
37575
TrEMBL
other Location (Reliability: 3)
D3JYW9_ACTDE
376
0
42505
TrEMBL
other Location (Reliability: 2)
A0A7C8ZX74_OPUST
377
0
42715
TrEMBL
other Location (Reliability: 2)
A0A5B6ZIZ4_DAVIN
342
0
38771
TrEMBL
other Location (Reliability: 2)
A0A7C9DWR9_OPUST
377
0
42707
TrEMBL
other Location (Reliability: 2)
A0A072UFI2_MEDTR
377
0
42543
TrEMBL
other Location (Reliability: 2)
M1WR17_PSEP2
Pseudodesulfovibrio piezophilus (strain DSM 21447 / JCM 15486 / C1TLV30)
324
0
36020
TrEMBL
-
A0A5B6ZFH6_DAVIN
376
0
42450
TrEMBL
other Location (Reliability: 2)
A0A1Z5KPK9_FISSO
362
0
40493
TrEMBL
other Location (Reliability: 1)
C6K2L0_SOLLC
376
0
42548
TrEMBL
other Location (Reliability: 2)
A0A5E6MPB3_9BACT
328
0
36525
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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
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
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
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Barber, G.A.; Hebda, P.A.
GDP-D-mannose:GDP-L-galactose epimerase from Chlorella pyrenoidosa
Methods Enzymol.
83
522-525
1982
Auxenochlorella pyrenoidosa
brenda
Goudsmit, E.M.; Neufeld, E.F.
Formation of GDP-L-galactose from GDP-D-mannose
Biochem. Biophys. Res. Commun.
26
730-735
1967
Helix pomatia
brenda
Hebda, P.A.; Behrman, E.J.; Barber, G.A.
The guanosine 5'-diphosphate D-mannose:guanosine 5'-diphosphate L-galactose epimerase of Chlorella pyrenoidosa
Arch. Biochem. Biophys.
194
496-502
1979
Auxenochlorella pyrenoidosa
brenda
Barber, G.A.
Observations on the mechanism of the reversible epimerization of GDP-D-mannose to GDP-L-galactose by an enzyme from Chlorella pyrenoidosa
J. Biol. Chem.
254
7600-7603
1979
Auxenochlorella pyrenoidosa
brenda
Wolucka, B.A.; Davey, M.W.; Boerjan, W.
A high-performance liquid chromatography radio method for determination of L-ascorbic acid and guanosine 5'-diphosphate-L-galactose, key metabolites of the plant vitamin C pathway
Anal. Biochem.
294
161-168
2001
Arabidopsis thaliana
brenda
Wolucka, B.A.; Van Montagu, M.
GDP-mannose 3',5'-epimerase forms GDP-L-gulose, a putative intermediate for the de novo biosynthesis of vitamin C in plants
J. Biol. Chem.
278
47483-47490
2003
Arabidopsis thaliana
brenda
Wolucka, B.A.; Persiau, G.; Van Doorsselaere, J.; Davey, M.W.; Demol, H.; Vandekerckhove, J.; Van Montagu, M.; Zabeau, M.; Boerjan, W.
Partial purification and identification of GDP-mannose 3",5"-epimerase of Arabidopsis thaliana, a key enzyme of the plant vitamin C pathway
Proc. Natl. Acad. Sci. USA
98
14843-14848
2001
Arabidopsis thaliana (Q93VR3), Arabidopsis thaliana
brenda
Major, L.L.; Wolucka, B.A.; Naismith, J.H.
Structure and function of GDP-mannose-3',5'-epimerase: an enzyme which performs three chemical reactions at the same active site
J. Am. Chem. Soc.
127
18309-18320
2005
Arabidopsis thaliana
brenda
Wolucka, B.A.; Goossens, A.; Inze, D.
Methyl jasmonate stimulates the de novo biosynthesis of vitamin C in plant cell suspensions
J. Exp. Bot.
56
527-2538
2005
Nicotiana tabacum
-
brenda
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
brenda
Gilbert, L.; Alhagdow, M.; Nunes-Nesi, A.; Quemener, B.; Guillon, F.; Bouchet, B.; Faurobert, M.; Gouble, B.; Page, D.; Garcia, V.; Petit, J.; Stevens, R.; Causse, M.; Fernie, A.R.; Lahaye, M.; Rothan, C.; Baldet, P.
GDP-D-mannose 3,5-epimerase (GME) plays a key role at the intersection of ascorbate and non-cellulosic cell-wall biosynthesis in tomato
Plant J.
60
499-508
2009
Solanum lycopersicum
brenda
Voxeur, A.; Gilbert, L.; Rihouey, C.; Driouich, A.; Rothan, C.; Baldet, P.; Lerouge, P.
Silencing of the GDP-D-mannose 3,5-epimerase affects the structure and cross-linking of the pectic polysaccharide rhamnogalacturonan II and plant growth in tomato
J. Biol. Chem.
286
8014-8020
2011
Solanum lycopersicum
brenda
Zhang, C.; Liu, J.; Zhang, Y.; Cai, X.; Gong, P.; Zhang, J.; Wang, T.; Li, H.; Ye, Z.
Overexpression of SlGMEs leads to ascorbate accumulation with enhanced oxidative stress, cold, and salt tolerance in tomato
Plant Cell Rep.
30
389-398
2011
Solanum lycopersicum (C6K2K9), Solanum lycopersicum (C6K2L0), Solanum lycopersicum
brenda
Yang, X.Y.; Xie, J.X.; Wang, F.F.; Zhong, J.; Liu, Y.Z.; Li, G.H.; Peng, S.A.
Comparison of ascorbate metabolism in fruits of two citrus species with obvious difference in ascorbate content in pulp
J. Plant Physiol.
168
2196-2205
2011
Citrus sinensis, Citrus unshiu (E9M5S1), Citrus unshiu
brenda
Li, J.; Cui, M.; Li, M.; Wang, X.; Liang, D.; Ma, F.
Expression pattern and promoter analysis of the gene encoding GDP-D-mannose 3',5'-epimerase under abiotic stresses and applications of hormones by kiwifruit
Sci. Hortic.
150
187-194
2013
Actinidia deliciosa (D3JYW9), Actinidia rufa (G1ETS7)
-
brenda
Chen, Y.; Bu, J.; Zhao, Z.; Zhao, J.; Liu, M.
Cloning and expression analysis of GDP-mannose-3,5-epimerase (ZjGME) from Ziziphus jujuba Mill
Acta Hortic.
1116
49-53
2016
Ziziphus jujuba
-
brenda
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