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Information on EC 1.1.1.8 - glycerol-3-phosphate dehydrogenase (NAD+) and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q00055
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1.1.1.8 glycerol-3-phosphate dehydrogenase (NAD+)IUBMB Comments
Also acts on propane-1,2-diol phosphate and glycerone sulfate (but with a much lower affinity).
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Word Map
- 1.1.1.8
- adipose
- adipocytes
- dhap
-
preadipocytes
-
alpha-gpdh
-
3-phosphatase
-
phosphodianion
-
fad-linked
- synthesis
- food industry
- nutrition
- medicine
- biotechnology
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
glycerol 3-phosphate dehydrogenase, mgpdh, gpdh-1, glycerol-3-phosphate dehydrogenase 1, gpd1p, g3p dehydrogenase, cgpdh, cggpd, gpdh-2, alpha glycerophosphate dehydrogenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-glycerol phosphate dehydrogenase (NAD)
-
-
-
-
alpha-glycerophosphate dehydrogenase (NAD)
-
-
-
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dehydrogenase, glycerol phosphate
-
-
-
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glycerol 1-phosphate dehydrogenase
-
-
-
-
glycerol phosphate dehydrogenase (NAD)
-
-
-
-
glycerophosphate dehydrogenase (NAD)
-
-
-
-
hydroglycerophosphate dehydrogenase
-
-
-
-
L-alpha-glycerol phosphate dehydrogenase
-
-
-
-
L-alpha-glycerophosphate dehydrogenase
-
-
-
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L-glycerol phosphate dehydrogenase
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-
-
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L-glycerophosphate dehydrogenase
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-
-
-
NAD-alpha-glycerophosphate dehydrogenase
-
-
-
-
NAD-dependent glycerol phosphate dehydrogenase
-
-
-
-
NAD-dependent glycerol-3-phosphate dehydrogenase
-
-
-
-
NAD-L-glycerol-3-phosphate dehydrogenase
-
-
-
-
NAD-linked glycerol 3-phosphate dehydrogenase
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-
-
-
NADH-dihydroxyacetone phosphate reductase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH + H+
equilibrium random-bi-bi reaction mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
sn-glycerol-3-phosphate:NAD+ 2-oxidoreductase
Also acts on propane-1,2-diol phosphate and glycerone sulfate (but with a much lower affinity).
CAS REGISTRY NUMBER
COMMENTARY
9075-65-4
-
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
dihydroxyacetone phosphate + NADH
glycerol-3-phosphate + NAD+
-
-
-
-
?
dihydroxyacetone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
-
-
-
?
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
-
?
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
?
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
oxidation at 3% the reaction rate of dihydroxyacetone phosphate reduction at pH 7.0
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
reverse reaction favoured direction
-
r
additional information
?
-
high NaCl tolerance seems to be determined by a combination of enhanced glycerol production, due to an increased expression of GPD1 (glycerol 3-phosphate dehydrogenase) and GPP2 (glycerol 3-phosphatase)
-
-
?
additional information
?
-
-
high NaCl tolerance seems to be determined by a combination of enhanced glycerol production, due to an increased expression of GPD1 (glycerol 3-phosphate dehydrogenase) and GPP2 (glycerol 3-phosphatase)
-
-
?
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
dihydroxyacetone phosphate + NADH
glycerol-3-phosphate + NAD+
-
-
-
-
?
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
-
?
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
glycerone phosphate + NADH + H+
-
-
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
-
-
?
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
oxidation at 3% the reaction rate of dihydroxyacetone phosphate reduction at pH 7.0
-
r
sn-glycerol 3-phosphate + NAD+
dihydroxyacetone phosphate + NADH + H+
-
reverse reaction favoured direction
-
r
additional information
?
-
high NaCl tolerance seems to be determined by a combination of enhanced glycerol production, due to an increased expression of GPD1 (glycerol 3-phosphate dehydrogenase) and GPP2 (glycerol 3-phosphatase)
-
-
?
additional information
?
-
-
high NaCl tolerance seems to be determined by a combination of enhanced glycerol production, due to an increased expression of GPD1 (glycerol 3-phosphate dehydrogenase) and GPP2 (glycerol 3-phosphatase)
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cl-
-
cations, i.e. H+, K+, Na+ associated with Cl- do not affect the reduction of dihydroxyacetone phosphate
fructose-1,6-bisphosphate
-
at physiological concentration, non-competitive
NAD+
-
competitive inhibitor to NADH at physiological concentration
phosphate
-
competitive inhibitor against dihydroxyacetone phosphate, non-competitive inhibitor against NADH
additional information
-
no inhibition by NADPH, acetaldehyde, glycerol, ethanol
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8
-
dihydroxyacetone reduction, activity decreases rapidly below pH 7.0 and above pH 8.0, more rapidly at acidic values
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
glycerol production rates of different strains, overview
additional information
glycerol production rates of different strains, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
isoform Gpd2p, contains mitochondrial presequence sufficient for targeting
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
evolution
structural and phylogenetic comparisons reveal four main structure types among the five families of glycerol-3-phosphate and glycerol-1-phosphate dehydrogenases, overview
evolution
Gpd1p from Saccharomyces kudriavzevii presented five conserved amino acid replacements compared to Saccharomyces cerevisiae (Ala31Ile, Ile67leu, Glu76Asp, Asp142Asn and Ser143Pro) out of 391 total residues, corresponding to an identity of 98.7%
metabolism
the interconversion of glycerol 3-phosphate and dihydroxyacetone phosphate by glycerol-3-phosphate dehydrogenases provides a link between carbohydrate and lipid metabolism. Glycerol 3-phosphate from the breakdown of phospholipids and triglycerides (via glycerol kinase) is converted into the glycolysis intermediate dihydroxyacetone phosphate, while the reverse reaction produces glycerol 3-phosphate, which is required for the synthesis of triglycerides and phospholipids
metabolism
Gpd1p is the flux controlling enzyme in the glycerol biosynthetic pathway
physiological function
the interconversion of glycerol 3-phosphate and dihydroxyacetone phosphate by glycerol-3-phosphate dehydrogenases provides Saccharomyces cerevisiae with protection against osmotic and anoxic stress. The concerted action of cytosolic (NAD+-dependent) G3PDHs and membrane-bound (FAD-dependent) G3PDHs transfers reducing equivalents from cytosolic NADH into the electron-transport chain of both bacteria and mitochondria
physiological function
Camelina sativa coexpressing Arabidopsis thaliana diacylglycerol acyltransferase1 (DGAT1) and yeast cytosolic glycerol-3-phosphate dehydrogenase (GPD1) genes exhibit up to 13% higher seed oil content and up to 52% increase in seed mass compared to wild-type plants. DGAT1- and GDP1-coexpressing lines show significantly higher seed and oil yields on a dry weight basis than the wild-type controls or plants expressing DGAT1 and GPD1 alone. The oil harvest index (g oil per g total dry matter) for DGTA1- and GPD1-coexpressing lines is almost twofold higher as compared to wild type and the lines expressing DGAT1 and GPD1 alone
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
31000
-
x * 31000, gel filtration, estimated from elution volume on sepharose 6B
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
-
x * 31000, gel filtration, estimated from elution volume on sepharose 6B
additional information
the enzyme monomer is organized with N- and C-terminal domains. The N-terminal domain contains a classic Rossmann fold with the (beta-alpha-beta-alpha-beta)2 motif typical of many NAD+-dependent enzymes, while the C-terminal domain is mainly alpha-helical, structure comparisons, overview
additional information
-
kinetic interaction between NADH dehydrogenases Nde1/Nde2 and enzyme isoform Gut2 at inner mitochondrial membrane
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant untagged enzyme, hanging drop vapour diffusion method using a reservoir solution consisting of 12% PEG 8000, 0.1 M Tris-HCl, pH 8.5, 0.3 M MgCl2, X-ray diffraction structure determination and analysis at 2.45 A resolution, molecular replacement and modeling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Deltagpd1
-
anaerobic growth, growth rate and glycerol production similar to wild-type
Deltagpd1/Deltacox18
-
anaerobic growth, growth rate and glycerol production similar to wild-type
Deltagpd2/Deltacox18
-
no growth under anaerobic or aerobic conditions
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in 0.1 M Tris-HCl, 2 mM 2-mercaptoethanol, pH 7.0, 50% polyethylene glycol 2000, 5 mM NADH or dihydroxyacetone phosphate, unstable
-
-80°C, in 0.1 M Tris-HCl, 2 mM 2-mercaptoethanol, pH 7.0, 50% polyethylene glycol 2000, 5 mM NADH or dihydroxyacetone phosphate, unstable
-
4°C, 1 M Tris-HCl, 2 mM 2-mercaptoethanol, pH 7.0, eluted from Sephadex G-100 column, 90% activity remained after several weeks
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4°C, stable for several weeks in 1 M Tris/HCl buffer with 2-mercaptoethanol, pH 7.0
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21 by anion exchange chromatography to over 95% purity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene YDL022W, phylogenetic analysis, expression in Escherichia coli strain BL21
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
there is significantly higher enzyme activity after osmotic (2.6, 5.2 and 3.6fold after 2, 4 and 8 h, respectively) and cold stresses (9.7, 19.9 and 2.2fold after 2, 4 and 8 h, respectively)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
potential use of Saccharomyces cerevisiae-Saccharomyces kudriavzevii hybrids in the wine industry where glycerol content is an important quality parameter
synthesis
biotechnology
-
deletion of the NAD+-dependent glycerol-3-phosphate dehydrogenase gene in an industrial ethanol-producing strain and expression of either the non-phosphorylating NADP+-dependent glyceraldehyde-3-phosphate dehydrogenase from Bacillus cereus, strain AG2A, or the NADP+-dependent glyceraldehyde-3-phosphate dehydrogenase GAPDH from Kluyveromyces lactis, strain AG2B, in the deletion strain. Recombinant strain AG2A exhibits a 48.70% decrease in glycerol production and a 7.60% increase in ethanol yield relative to the amount of substrate consumed, while recombinant strain AG2B exhibits a 52.90% decrease in glycerol production and a 7.34% increase in ethanol yield relative to the amount of substrate consumed, compared with the wild-type strain. The maximum specific growth rates of the recombinant AG2A and AG2B are higher than that of the gpd2 deletion strain and are indistinguishable compared with the wild-type strain in anaerobic batch fermentations
nutrition
-
yeast strains overexpressing glycerol-3-phosphate dehydrogenase may be used to produce wine with decreased ethanol content
synthesis
synthesis
Camelina sativa coexpressing Arabidopsis thaliana diacylglycerol acyltransferase1 (DGAT1) and yeast cytosolic glycerol-3-phosphate dehydrogenase (GPD1) genes exhibit up to 13% higher seed oil content and up to 52% increase in seed mass compared to wild-type plants. DGAT1- and GDP1-coexpressing lines show significantly higher seed and oil yields on a dry weight basis than the wild-type controls or plants expressing DGAT1 and GPD1 alone. The oil harvest index (g oil per g total dry matter) for DGTA1- and GPD1-coexpressing lines is almost twofold higher as compared to wild type and the lines expressing DGAT1 and GPD1 alone
synthesis
upon heterologous expression of diacylglycerol acyltransferase DGAT1, glycerol-3-phosphate dehydrogenase GPD1 and DGAT1 + GPD1 in Camelina sativa, increase in triacylglycerol production is limited by utilization of fixed carbon from the source tissues supported by the increase in glycolysis pathway metabolites and decreased transcripts levels of transcription factors controlling fatty acids synthesis, and triacylglycerol accumulation is limited by the activity of lipases/hydrolases that hydrolyze triacylglycerol pool supported by the increase in free fatty acids and monoacylglycerols
synthesis
-
fermentative production of L-glycerol 3-phosphate utilizing a Saccharomyces cerevisiae strain with an engineered glycerol biosynthetic pathway (strain with deletions in both genes encoding specific L-G3Pases (GPP1 and GPP2) and multicopy overexpression of L-glycerol 3-phosphate dehydrogenase). Up-scaling the process employs fed-batch fermentation with repeated glucose feeding, plus an aerobic growth phase followed by an anaerobic product accumulation phase. This produces a final product titer of about 325 mg total L-glycerol 3-phosphate per liter of fermentation broth
synthesis
-
successful introduction of a glycerol production pathway into Klebseiella pneumoniae by coexpression of genes encoding glycerol-3-phosphate dehydrogenase and glycerol-3-phosphatase (EC 3.1.3.21) organized into the plasmid pUC18K under control of the respective lac promoter. An engineered Klebsiella pneumoniae that can produce glycerol from glucose is achieved. It is still difficult to efficiently produce 1,3-propanediol from glucose. Only 0.58 g/l 1,3-propanediol is produced
synthesis
-
deletion of the NAD+-dependent glycerol-3-phosphate dehydrogenase gene in an industrial ethanol-producing strain and expression of either the non-phosphorylating NADP+-dependent glyceraldehyde-3-phosphate dehydrogenase from Bacillus cereus, strain AG2A, or the NADP+-dependent glyceraldehyde-3-phosphate dehydrogenase GAPDH from Kluyveromyces lactis, strain AG2B, in the deletion strain. Recombinant strain AG2A exhibits a 48.70% decrease in glycerol production and a 7.60% increase in ethanol yield relative to the amount of substrate consumed, while recombinant strain AG2B exhibits a 52.90% decrease in glycerol production and a 7.34% increase in ethanol yield relative to the amount of substrate consumed, compared with the wild-type strain. The maximum specific growth rates of the recombinant AG2A and AG2B are higher than that of the gpd2 deletion strain and are indistinguishable compared with the wild-type strain in anaerobic batch fermentations
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Albertyn, J.; Van Tonder, A.; Prior, B.A.
Purification and characterization of glycerol-3-phosphate dehydrogenase of Saccharomyces cerevisiae
FEBS Lett.
308
130-132
1992
Saccharomyces cerevisiae, Saccharomyces cerevisiae H44-3D
Merkel, J.R.; Straume, M.; Sajer, S.A.; Hopfer, R.L.
Purification and some properties of sn-glycerol-3-phosphate dehydrogenase from Saccharomyces cerevisiae
Anal. Biochem.
122
180-185
1982
Saccharomyces cerevisiae
Cai, J.; Pietzsch, M.; Theobald, U.; Rizzi, M.
Fast purification and kinetic studies of the glycerol-3-phosphate dehydrogenase from the yeast Saccharomyces cerevisiae
Biotechnology
49
19-27
1996
Saccharomyces cerevisiae, Saccharomyces cerevisiae YSH 11-6B
Pahlman, I.L.; Larsson, C.; Averet, N.; Bunoust, O.; Boubekeur, S.; Gustafsson, L.; Rigoulet, M.
Kinetic regulation of the mitochondrial glycerol-3-phosphate dehydrogenase by the external NADH dehydrogenase in Saccharomyces cerevisiae
J. Biol. Chem.
277
27991-27995
2002
Saccharomyces cerevisiae
Valadi, A.; Granath, K.; Gustafsson, L.; Adler, L.
Distinct intracellular localization of Gpd1p and Gpd2p, the two yeast isoforms of NAD+-dependent glycerol-3-phosphate dehydrogenase, explains their different contributions to redox-driven glycerol production
J. Biol. Chem.
279
39677-39685
2004
Saccharomyces cerevisiae
Gori, K.; Mortensen, H.D.; Arneborg, N.; Jespersen, L.
Expression of the GPD1 and GPP2 orthologues and glycerol retention during growth of Debaryomyces hansenii at high NaCl concentrations
Yeast
22
1213-1222
2005
Saccharomyces cerevisiae (Q00055), Saccharomyces cerevisiae, Debaryomyces hansenii (Q6VPR1), Debaryomyces hansenii
Cambon, B.; Monteil, V.; Remize, F.; Camarasa, C.; Dequin, S.
Effects of GPD1 overexpression in Saccharomyces cerevisiae commercial wine yeast strains lacking ALD6 genes
Appl. Environ. Microbiol.
72
4688-4694
2006
Saccharomyces cerevisiae
Popp, A.; Nguyen, H.T.; Boulahya, K.; Bideaux, C.; Alfenore, S.; Guillouet, S.E.; Nevoigt, E.
Fermentative production of L-glycerol 3-phosphate utilizing a Saccharomyces cerevisiae strain with an engineered glycerol biosynthetic pathway
Biotechnol. Bioeng.
100
497-505
2008
Saccharomyces cerevisiae
Zheng, Y.; Zhao, L.; Zhang, J.; Zhang, H.; Ma, X.; Wei, D.
Production of glycerol from glucose by coexpressing glycerol-3-phosphate dehydrogenase and glycerol-3-phosphatase in Klebsiella pneumoniae
J. Biosci. Bioeng.
105
508-512
2008
Saccharomyces cerevisiae, Saccharomyces cerevisiae Y47
Guo, Z.P.; Zhang, L.; Ding, Z.Y.; Wang, Z.X.; Shi, G.Y.
Improving ethanol productivity by modification of glycolytic redox factor generation in glycerol-3-phosphate dehydrogenase mutants of an industrial ethanol yeast
J. Ind. Microbiol. Biotechnol.
38
935-943
2011
Saccharomyces cerevisiae
Alarcon, D.A.; Nandi, M.; Carpena, X.; Fita, I.; Loewen, P.C.
Structure of glycerol-3-phosphate dehydrogenase (GPD1) from Saccharomyces cerevisiae at 2.45 A resolution
Acta Crystallogr. Sect. F
68
1279-1283
2012
Saccharomyces cerevisiae (Q00055)
Guadalupe-Medina, V.; Metz, B.; Oud, B.; van Der Graaf, C.M.; Mans, R.; Pronk, J.T.; van Maris, A.J.
Evolutionary engineering of a glycerol-3-phosphate dehydrogenase-negative, acetate-reducing Saccharomyces cerevisiae strain enables anaerobic growth at high glucose concentrations
Microb. Biotechnol.
7
44-53
2014
Saccharomyces cerevisiae, Saccharomyces cerevisiae IME076
Oliveira, B.M.; Barrio, E.; Querol, A.; Perez-Torrado, R.
Enhanced enzymatic activity of glycerol-3-phosphate dehydrogenase from the cryophilic Saccharomyces kudriavzevii
PLoS ONE
9
e87290
2014
Saccharomyces cerevisiae, Saccharomyces cerevisiae (Q00055), Saccharomyces cerevisiae BY4741, Saccharomyces kudriavzevii, Saccharomyces kudriavzevii (A0A060KZ16), Saccharomyces kudriavzevii IFO1802
Chhikara, S.; Abdullah, H.M.; Akbari, P.; Schnell, D.; Dhankher, O.P.
Engineering Camelina sativa (L.) Crantz for enhanced oil and seed yields by combining diacylglycerol acyltransferase1 and glycerol-3-phosphate dehydrogenase expression
Plant Biotechnol. J.
16
1034-1045
2018
Saccharomyces cerevisiae (Q00055), Saccharomyces cerevisiae ATCC 204508 (Q00055)
Abdullah, H.M.; Chhikara, S.; Akbari, P.; Schnell, D.J.; Pareek, A.; Dhankher, O.P.
Comparative transcriptome and metabolome analysis suggests bottlenecks that limit seed and oil yields in transgenic Camelina sativa expressing diacylglycerol acyltransferase 1 and glycerol-3-phosphate dehydrogenase
Biotechnol. Biofuels
11
335
2018
Saccharomyces cerevisiae (Q00055), Saccharomyces cerevisiae ATCC 204508 (Q00055)
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