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1-palmitoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-palmitoleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
1-stearoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-oleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
a 1-stearoyl-2-acyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a 1-oleoyl-2-acyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
1-palmitoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-palmitoleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1-palmitoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-palmitoleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1-stearoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-oleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
-
?
1-stearoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-oleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1-stearoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-oleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1-stearoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-oleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1-stearoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-oleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1-stearoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-oleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
-
?
1-stearoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-oleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
Thermostichus vulcanus
-
-
-
-
?
1-stearoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-oleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
Thermostichus vulcanus
-
-
-
?
1-stearoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-oleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1-stearoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-oleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
a 1-stearoyl-2-acyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a 1-oleoyl-2-acyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
-
?
a 1-stearoyl-2-acyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a 1-oleoyl-2-acyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
?
a 1-stearoyl-2-acyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a 1-oleoyl-2-acyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
the enzyme does not desaturate palmitic acid, palmitoleic acid, and cis-vaccenic acid
-
-
?
a 1-stearoyl-2-acyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a 1-oleoyl-2-acyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
?
a 1-stearoyl-2-acyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a 1-oleoyl-2-acyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
the enzyme does not desaturate palmitic acid, palmitoleic acid, and cis-vaccenic acid
-
-
?
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1-palmitoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-palmitoleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
1-stearoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-oleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
a 1-stearoyl-2-acyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a 1-oleoyl-2-acyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
1-palmitoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-palmitoleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1-palmitoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-palmitoleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1-stearoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-oleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
-
?
1-stearoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-oleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1-stearoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-oleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1-stearoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-oleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1-stearoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-oleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1-stearoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-oleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
-
?
1-stearoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-oleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
Thermostichus vulcanus
-
-
-
-
?
1-stearoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-oleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
Thermostichus vulcanus
-
-
-
?
1-stearoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-oleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1-stearoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-oleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
a 1-stearoyl-2-acyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a 1-oleoyl-2-acyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
?
a 1-stearoyl-2-acyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
a 1-oleoyl-2-acyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
?
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Carcinogenesis
DESC1, a novel tumor suppressor, sensitizes cells to apoptosis by down-regulating the EGFR/AKT pathway in esophageal squamous cell carcinoma.
Carcinoma
Crystal structure of the catalytic domain of DESC1, a new member of the type II transmembrane serine proteinase family.
Carcinoma
DESC1, a novel tumor suppressor, sensitizes cells to apoptosis by down-regulating the EGFR/AKT pathway in esophageal squamous cell carcinoma.
Carcinoma
Differential expression of a novel serine protease homologue in squamous cell carcinoma of the head and neck.
Carcinoma
Expression of the serine protease DESC1 correlates directly with normal keratinocyte differentiation and inversely with head and neck squamous cell carcinoma progression.
Carcinoma
Human DESC1 serine protease confers tumorigenic properties to MDCK cells and it is upregulated in tumours of different origin.
Carcinoma
LncRNA LOXL1-AS1 promotes esophageal squamous cell carcinoma progression by targeting DESC1.
Carcinoma
LncRNA-TUSC7/miR-224 affected chemotherapy resistance of esophageal squamous cell carcinoma by competitively regulating DESC1.
Carcinoma, Squamous Cell
Crystal structure of the catalytic domain of DESC1, a new member of the type II transmembrane serine proteinase family.
Carcinoma, Squamous Cell
Differential expression of a novel serine protease homologue in squamous cell carcinoma of the head and neck.
Carcinoma, Squamous Cell
Expression of the serine protease DESC1 correlates directly with normal keratinocyte differentiation and inversely with head and neck squamous cell carcinoma progression.
Carcinoma, Squamous Cell
Human DESC1 serine protease confers tumorigenic properties to MDCK cells and it is upregulated in tumours of different origin.
Coronavirus Infections
DESC1 and MSPL activate influenza A viruses and emerging coronaviruses for host cell entry.
Esophageal Squamous Cell Carcinoma
DESC1, a novel tumor suppressor, sensitizes cells to apoptosis by down-regulating the EGFR/AKT pathway in esophageal squamous cell carcinoma.
Esophageal Squamous Cell Carcinoma
LncRNA LOXL1-AS1 promotes esophageal squamous cell carcinoma progression by targeting DESC1.
Esophageal Squamous Cell Carcinoma
LncRNA-TUSC7/miR-224 affected chemotherapy resistance of esophageal squamous cell carcinoma by competitively regulating DESC1.
Influenza, Human
DESC1 and MSPL activate influenza A viruses and emerging coronaviruses for host cell entry.
Neoplasms
Crystal structure of the catalytic domain of DESC1, a new member of the type II transmembrane serine proteinase family.
Neoplasms
DESC1, a novel tumor suppressor, sensitizes cells to apoptosis by down-regulating the EGFR/AKT pathway in esophageal squamous cell carcinoma.
Neoplasms
Human DESC1 serine protease confers tumorigenic properties to MDCK cells and it is upregulated in tumours of different origin.
Severe Acute Respiratory Syndrome
DESC1 and MSPL activate influenza A viruses and emerging coronaviruses for host cell entry.
Squamous Cell Carcinoma of Head and Neck
Expression of the serine protease DESC1 correlates directly with normal keratinocyte differentiation and inversely with head and neck squamous cell carcinoma progression.
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metabolism
desaturases, key enzymes in the metabolism of fatty acids, regulate the physical and biochemical properties of membranes. They adjust the composition of saturated and unsaturated fatty acids in response to changes in the environmental. This DELTA9-desaturation reaction normally requires molecular oxygen and reducing equivalents derived from NAD(P)H through an electron system consisting of either NADPH, cytochrome b5 and cytochrome b5-reductase in animals and fungi or ferredoxin-NADP+ oxidoreductase and ferredoxin in bacteria and plants
metabolism
the enzyme is involved in fatty acid desaturation in metabolism, overview
metabolism
-
desaturases, key enzymes in the metabolism of fatty acids, regulate the physical and biochemical properties of membranes. They adjust the composition of saturated and unsaturated fatty acids in response to changes in the environmental. This DELTA9-desaturation reaction normally requires molecular oxygen and reducing equivalents derived from NAD(P)H through an electron system consisting of either NADPH, cytochrome b5 and cytochrome b5-reductase in animals and fungi or ferredoxin-NADP+ oxidoreductase and ferredoxin in bacteria and plants
-
physiological function
Thermostichus vulcanus
-
at optimum growth temperature, a decreased number of grana and thylakoids and an increased number of plastoglobules and their larger area are observed in desC-transgenic plants when compared to control plants. Transgenic plants respond to cold by reducing the chloroplast, granal and plastoglobule areas
physiological function
Thermostichus vulcanus
-
the activity of antioxidant enzymes in the desC-transgenic plants depends on the operation of the introduced desC gene for acyl-lipid DELTA9-desaturase. Its activity results in an increase in the relative content of polyunsaturated fatty acids in the membrane lipids ensuring the liquid state of membranes during chilling. DesC-transgenic plants maintain a higher activity of antioxidant enzymes during 2 h incubation at 2°C. As a result, these plants resist more efficiently the accumulation of reactive oxygen species and reduce the rate of the lipid peroxidation
physiological function
Thermostichus vulcanus
-
the expression of acyl-lipid DELTA9-desaturase in tobacco plants results in the lower number of grana and thylakoids in a chloroplast in parallel with an increased number of plastoglobules and their larger area
physiological function
the D9-fatty acid desaturase initiates the synthesis of polyunsaturated fatty acids by introducing the first double bond at the C9 position of saturated fatty acid chains. These substrates can further be elongated by other classes of desaturase enzymes
physiological function
the enzyme plays a critical role in the metabolism of the parasite
physiological function
-
the D9-fatty acid desaturase initiates the synthesis of polyunsaturated fatty acids by introducing the first double bond at the C9 position of saturated fatty acid chains. These substrates can further be elongated by other classes of desaturase enzymes
-
physiological function
-
the enzyme plays a critical role in the metabolism of the parasite
-
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DNA and amino acid sequence determination and analysis, functional overexpression of His6-tagged enzyme in Escherichia coli strain BL21 codon Plus, subcloning in Escherichia coli strain XL 10 GOLD, TcDELTA9DES-expressing Escherichia coli cells exhibit high desaturase activity associated with increased levels of monounsaturated fatty acids. The fatty acid composition of Escherichia coli shows that the recombinant desaturase can use 16:0 as substrate
expressed in Escherichia coli
Thermostichus vulcanus
expressed in Nicotiana tabacum
Thermostichus vulcanus
-
expressed in Nicotiana tabacum leaves
Thermostichus vulcanus
-
expressed in Saccharomyces cerevisiae strain AMY2alpha
expression in Escherichia coli
gene desC1, DNA and amino acid sequence determination, phylogenetic analysis
gene PA3FAD9, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, functional recombinant expression in Escherichia coli, GCMS analysis reveals that palmitoleic (C16:1DELTA9) and oleic acids (C18:1DELTA9) are the only unsaturated fatty acids identified in addition to the endogenous fatty acids, expression at 15°C
gene PA8FAD9, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli strain Transetta (DE3), ability of the enzyme to convert exogenous stearic acid to oleic acid incorporated into the recombinant Escherichia coli membrane phospholipids. GCMS analysis confirms significant changes in the pattern of palmitoleic and palmitic acid production in Escherichia coli cells expressing PA8FAD9 gene. At 20°C, the amount of palmitoleic increased from 10.5 to 21% suggesting that PA8FAD9 gene from Pseudomonas sp. A8 codes for an active DELTA9-fatty acid desaturase-like protein
recombinant expression of hybrid gene of Synechococcus vulcanus DELTA9 (desC) acyl-lipid desaturase in Nicotiana tabacum cv. Wisconsin, as chimeric enzyme DesC-LicBM3 with reporter thermostable lichenase of Clostridium thermocellum, expression with or without the sequence coding for transit peptide of Rubisco small subunit of Arabidopsis thaliana under control of the 35S CaMV constitutive promoter using the Agrobacterium tumefaciens strain GV3101-mediated transformation method, measurement of recombinant lichenase activity. Plants expressing RTP::desC::licBM3 gene coding for DELTA9 desaturase with the transit pepride for transport into chloroplasts exhibit a significant increase of alpha-linolenic acid (DELTA9,12,15-18:3) portion accompanied by decrease of DELTA9,12-18:2 level while the part of the third major fatty acid, palmitic acid, remains unchanged
Thermostichus vulcanus
expression in Escherichia coli
expression in Escherichia coli
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Sakamoto, T.; Wada, H.; Nishida, I.; Ohmori, M.; Murata, N.
DELTA9 Acyl-lipid desaturases of cyanobacteria. Molecular cloning and substrate specificities in terms of fatty acids, sn-positions, and polar head groups
J. Biol. Chem.
269
25576-25580
1994
Synechocystis sp. (Q79F68), Trichormus variabilis (Q79F73)
brenda
Higashi, S.; Murata, N.
An in vivo study of substrate specificities of acyl-lipid desaturases and acyltransferases in lipid synthesis in Synechocystis PCC6803
Plant Physiol.
102
1275-1278
1993
Synechocystis sp.
brenda
Meesapyodsuk, D.; Reed, D.W.; Cheevadhanarak, S.; Deshnium, P.; Covello, P.S.
Probing the mechanism of a cyanobacterial Delta9 fatty acid desaturase from Spirulina platensis C1 (Arthrospira sp. PCC 9438)
Comp. Biochem. Physiol. B
129
831-835
2001
Arthrospira platensis (O33722), Arthrospira platensis C1 (O33722)
brenda
Sakamoto, T.; Higashi, S.; Wada, H.; Murata, N.; Bryant, D.A.
Low-temperature-induced desaturation of fatty acids and expression of desaturase genes in the cyanobacterium Synechococcus sp. PCC 7002
FEMS Microbiol. Lett.
152
313-320
1997
Synechococcus sp.
brenda
Kiseleva, L.L.; Serebriiskaya, T.S.; Horvath, I.; Vigh, L.; Lyukevich, A.A.; Los, D.A.
Expression of the gene for the DELTA9 acyl-lipid desaturase in the thermophilic cyanobacterium
J. Mol. Microbiol. Biotechnol.
2
331-338
2000
Thermostichus vulcanus (Q9ZAP7)
brenda
Fukuchi-Mizutani, M.; Tasaka, Y.; Tanaka, Y.; Ashikari, T.; Kusumi, T.; Murata, N.
Characterization of DELTA9 acyl-lipid desaturase homologues from Arabidopsis thaliana
Plant Cell Physiol.
39
247-253
1998
Arabidopsis thaliana
brenda
Popov, V.; Orlova, I.; Kipaikina, N.; Serebriiskaya, T.; Merkulova, N.; Nosov, A.; Trunova, T.; Tsydendambaev, V.; Los, D.
The effect of tobacco plant transformation with a gene for acyl-lipid DELTA9-desaturase from Synechococcus vulcanus on plant chilling tolerance
Russ. J. Plant Physiol.
52
664-667
2005
Thermostichus vulcanus
-
brenda
Popov, V.; Kipaikina, N.; Astakhova, N.; Trunova, T.
Specific features of oxidative stress in the chilled tobacco plants following transformation with the desC gene for acyl-lipid DELTA9-desaturase from Synechococcus vulcanus
Russ. J. Plant Physiol.
53
469-473
2006
Thermostichus vulcanus
-
brenda
Popov, V.; Kipaikina, N.; Astakhova, N.; Trunova, T.
Chloroplast ultrastructure in leaves of tobacco plants with the introduced gene for the acyl-lipid DELTA9-desaturase from Synechococcus vulcanus at normal and low temperature
Russ. J. Plant Physiol.
54
278-281
2007
Thermostichus vulcanus
-
brenda
Sinetova, M.A.; Bolatkhan, K.; Sidorov, R.A.; Mironov, K.S.; Skrypnik, A.N.; Kupriyanova, E.V.; Zayadan, B.K.; Shumskaya, M.; Los, D.A.
Polyphasic characterization of the thermotolerant cyanobacterium Desertifilum sp. strain IPPAS B-1220
FEMS Microbiol. Lett.
364
doi: 10.1093/femsle/fnx027
2017
Desertifilum sp. IPPAS B-1220 (A0A1E5QD81)
brenda
Woelke, M.R.; Paulucci, N.S.; Selva, A.; Garban, H.; de Lema, M.G.
DELTA9 desaturase from Trypanosoma cruzi key enzyme in the parasite metabolism. Cloning and overexpression
Microbiol. Res.
194
29-37
2017
Trypanosoma cruzi (G8FL60), Trypanosoma cruzi Tulahuen (G8FL60)
brenda
Garba, L.; Ali, M.S.; Oslan, S.N.; Rahman, R.N.
Heterologous expression of PA8FAD9 and functional characterization of a DELTA9-fatty acid desaturase from a cold-tolerant Pseudomonas sp. A8
Mol. Biotechnol.
58
718-728
2016
Pseudomonas sp. (A0A165DNG6), Pseudomonas sp., Pseudomonas sp. A8(2016b) (A0A165DNG6)
brenda
Garba, L.; Mohamad Ali, M.S.; Oslan, S.N.; Rahman, R.N.
Molecular cloning and functional expression of a DELTA9-fatty acid desaturase from an antarctic Pseudomonas sp. A3
PLoS ONE
11
e0160681
2016
Pseudomonas sp. (A0A0S1Z203), Pseudomonas sp., Pseudomonas sp. A3(2015c) (A0A0S1Z203)
brenda
Gerasymenko, I.; Sakhno, L.; Kyrpa, T.; Ostapchuk, A.; Hadjiev, T.; Goldenkova-Pavlova, I.; Sheludko, Y.
Characterization of Nicotiana tabacum plants expressing hybrid genes of cyanobacterial DELTA9 or DELTA12 acyl-lipid desaturases and thermostable lichenase
Russ. J. Plant Physiol.
62
283-291
2015
Thermostichus vulcanus (Q9ZAP7)
-
brenda