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(2S,3S)-2,3-butanediol + NAD+
(3S)-acetoin + NADH + H+
-
-
-
-
r
(3S)-acetoin + NADH + H+
(2S,3S)-2,3-butanediol + NAD+
-
97% of the activity with diacetyl
97.3% enantiomeric excess and 96.5% diastereomeric excess
-
r
1,2-propanediol + NAD+
? + NADH + H+
-
-
0.5% of the activity with 2,3-butanediol
-
r
2,3-hexanedione + NADH + H+
? + NAD+
-
-
66% of the activity with diacetyl
-
?
2,3-pentanedione + beta-NADH + H+
L-3-hydroxy-2-pentanone + beta-NAD+
-
-
-
-
ir
2,3-pentanedione + NADH + H+
3-hydroxy-2-pentanone + NAD+
2,3-pentanedione + NADH + H+
? + NAD+
-
-
69% of the activity with diacetyl
-
?
3,4-hexanedione + NADH + H+
? + NAD+
-
-
10% of the activity with diacetyl
-
?
diacetyl + beta-NADH + H+
(S)-acetoin + beta-NAD+
-
86.9% of the activity with pentane-2,3-dione
-
-
ir
diacetyl + NADH + H+
(3S)-acetoin + NAD+
-
-
97.3% enantiomeric excess
-
ir
diacetyl + NADH + H+
(R)-acetoin + NAD+
diacetyl + NADH + H+
(S)-acetoin + NAD+
diacetyl + NADPH + H+
(S)-acetoin + NADP+
ethyl pyruvate + beta-NADH + H+
? + beta-NAD+
-
38.4% of the activity with pentane-2,3-dione
-
-
ir
ethyl pyruvate + NADH + H+
? + NAD+
-
57.7% of the activity with diacetyl
-
-
?
methyl glyoxal + NADH + H+
? + NAD+
-
11% of the activity with diacetyl
-
-
?
methyl pyruvate + beta-NADH + H+
? + beta-NAD+
-
22.8% of the activity with pentane-2,3-dione
-
-
ir
methyl pyruvate + NADH + H+
? + NAD+
-
49% of the activity with diacetyl
-
-
?
additional information
?
-
2,3-pentanedione + NADH + H+
3-hydroxy-2-pentanone + NAD+
-
85.6% of the activity with diacetyl
-
-
?
2,3-pentanedione + NADH + H+
3-hydroxy-2-pentanone + NAD+
77% of the (R)-2,3-butanediol dehydrogenase activity with substrate acetoin
-
-
?
diacetyl + NADH + H+
(R)-acetoin + NAD+
-
-
-
r
diacetyl + NADH + H+
(R)-acetoin + NAD+
-
-
-
r
diacetyl + NADH + H+
(S)-acetoin + NAD+
-
-
-
-
?
diacetyl + NADH + H+
(S)-acetoin + NAD+
-
-
-
-
?
diacetyl + NADH + H+
(S)-acetoin + NAD+
-
-
-
-
ir
diacetyl + NADH + H+
(S)-acetoin + NAD+
-
-
-
-
?
diacetyl + NADH + H+
(S)-acetoin + NAD+
-
-
-
-
?
diacetyl + NADH + H+
(S)-acetoin + NAD+
-
-
-
?
diacetyl + NADH + H+
(S)-acetoin + NAD+
-
-
-
r
diacetyl + NADH + H+
(S)-acetoin + NAD+
stereospecific reaction
-
-
?
diacetyl + NADH + H+
(S)-acetoin + NAD+
87% of the (R)-2,3-butanediol dehydrogenase activity with substrate acetoin
-
-
?
diacetyl + NADH + H+
(S)-acetoin + NAD+
-
-
-
?
diacetyl + NADH + H+
(S)-acetoin + NAD+
-
-
-
?
diacetyl + NADH + H+
(S)-acetoin + NAD+
-
-
-
?
diacetyl + NADH + H+
(S)-acetoin + NAD+
-
-
-
r
diacetyl + NADH + H+
(S)-acetoin + NAD+
-
-
-
?
diacetyl + NADH + H+
(S)-acetoin + NAD+
-
-
-
-
r
diacetyl + NADH + H+
(S)-acetoin + NAD+
-
-
-
?
diacetyl + NADPH + H+
(S)-acetoin + NADP+
-
-
-
-
ir
diacetyl + NADPH + H+
(S)-acetoin + NADP+
KC505218
-
-
-
ir
diacetyl + NADPH + H+
(S)-acetoin + NADP+
KC505218
-
-
-
ir
additional information
?
-
-
enzyme shows oxidative activity to racemic 2,3-butanediol but no activity toward racemic acetoin in the presence of NAD+
-
-
?
additional information
?
-
-
the enzyme shows an S-enantioselectivity in the reversible reduction of acetoin so it might be responsible of the meso-butenediol formation from R-acetoin. It acts on racemic acetoin and (S)-acetoin to form (2S,3S)-butane-2,3-diol, EC 1.1.1.76, but also on the (2R,3R)-butane-2,3-diol isomer in the reverse reaction, EC 1.1.1.4
-
-
?
additional information
?
-
-
the enzyme shows an S-enantioselectivity in the reversible reduction of acetoin so it might be responsible of the meso-butenediol formation from R-acetoin. It acts on racemic acetoin and (S)-acetoin to form (2S,3S)-butane-2,3-diol, EC 1.1.1.76, but also on the (2R,3R)-butane-2,3-diol isomer in the reverse reaction, EC 1.1.1.4
-
-
?
additional information
?
-
KpDAR has clear activities towards diacetyl, (R)/(S)-acetoin (cf. EC 1.1.1.303) and meso-2,3-butanediol with NADH/NAD+ as the cofactor. Diacetyl is the best substrate in the ketone reduction reactions. meso-2,3-Butanediol is the best substrate in the alcohol oxidation reactions, while very low activity is observed with (R)/(S)-acetoin, (2S,3S)-2,3-butanediol (EC 1.1.1.76) and (2R,3R)-2,3-butanediol (EC 1.1.1.4). Optimization of the reaction conditions, overview. Chiral-column GC analyses of products produced by whole-cells of recombinant Escherichia coli
-
-
-
additional information
?
-
the enzyme BudC also catalyzes the reduction of acetoin by NADH, cf. EC 1.1.1.76
-
-
-
additional information
?
-
enzyme shows activity as a reductase specific for (S)-acetoin, EC 1.1.1.76, and both diacetyl reductase (EC 1.1.1.304) and NAD+-dependent alcohol dehydrogenase (EC 1.1.1.1) activities
-
-
?
additional information
?
-
-
enzyme shows activity as a reductase specific for (S)-acetoin, EC 1.1.1.76, and both diacetyl reductase (EC 1.1.1.304) and NAD+-dependent alcohol dehydrogenase (EC 1.1.1.1) activities
-
-
?
additional information
?
-
KC505218
the enzyme also catalyzes the stereospcific reaction of (S)-acetoin reduction to butanediol, EC 1.1.1.76
-
-
?
additional information
?
-
-
the enzyme also catalyzes the stereospcific reaction of (S)-acetoin reduction to butanediol, EC 1.1.1.76
-
-
?
additional information
?
-
KC505218
the enzyme also catalyzes the stereospcific reaction of (S)-acetoin reduction to butanediol, EC 1.1.1.76
-
-
?
additional information
?
-
-
the enzyme also catalyzes the stereospcific reaction of (S)-acetoin reduction to butanediol, EC 1.1.1.76
-
-
?
additional information
?
-
-
Rhodococcus erythropolis WZ010 is capable of producing optically pure (2S,3S)-2,3-butanediol in alcoholic fermentation.
-
-
?
additional information
?
-
Rhodococcus erythropolis WZ010 is capable of producing optically pure (2S,3S)-2,3-butanediol in alcoholic fermentation.
-
-
?
additional information
?
-
-
the enzyme displays absolute stereospecificity in the reduction of diacetyl to (2S,3S)-2,3-butanediol via (S)-acetoin. The enzyme shows higher catalytic efficiency for (S)-1-phenylethanol oxidation than that for acetophenone reduction. ReADR-catalyzed asymmetric reduction of diacetyl is coupled with stereoselective oxidation of 1-phenylethanol, which simultaneously forms both (2S,3S)-2,3-butanediol and (R)-1-phenylethanol in great conversions and enantiomeric excess values.The enzyme accepts a broad range of substrates including aliphatic and aryl alcohols, aldehydes, and ketones
-
-
?
additional information
?
-
the enzyme displays absolute stereospecificity in the reduction of diacetyl to (2S,3S)-2,3-butanediol via (S)-acetoin. The enzyme shows higher catalytic efficiency for (S)-1-phenylethanol oxidation than that for acetophenone reduction. ReADR-catalyzed asymmetric reduction of diacetyl is coupled with stereoselective oxidation of 1-phenylethanol, which simultaneously forms both (2S,3S)-2,3-butanediol and (R)-1-phenylethanol in great conversions and enantiomeric excess values.The enzyme accepts a broad range of substrates including aliphatic and aryl alcohols, aldehydes, and ketones
-
-
?
additional information
?
-
-
Rhodococcus erythropolis WZ010 is capable of producing optically pure (2S,3S)-2,3-butanediol in alcoholic fermentation.
-
-
?
additional information
?
-
-
the enzyme displays absolute stereospecificity in the reduction of diacetyl to (2S,3S)-2,3-butanediol via (S)-acetoin. The enzyme shows higher catalytic efficiency for (S)-1-phenylethanol oxidation than that for acetophenone reduction. ReADR-catalyzed asymmetric reduction of diacetyl is coupled with stereoselective oxidation of 1-phenylethanol, which simultaneously forms both (2S,3S)-2,3-butanediol and (R)-1-phenylethanol in great conversions and enantiomeric excess values.The enzyme accepts a broad range of substrates including aliphatic and aryl alcohols, aldehydes, and ketones
-
-
?
additional information
?
-
-
no activity with alpha-NADH or NADPH
-
-
?
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diacetyl + NADH + H+
(R)-acetoin + NAD+
diacetyl + NADH + H+
(S)-acetoin + NAD+
additional information
?
-
diacetyl + NADH + H+
(R)-acetoin + NAD+
-
-
-
r
diacetyl + NADH + H+
(R)-acetoin + NAD+
-
-
-
r
diacetyl + NADH + H+
(S)-acetoin + NAD+
-
-
-
-
?
diacetyl + NADH + H+
(S)-acetoin + NAD+
-
-
-
-
?
diacetyl + NADH + H+
(S)-acetoin + NAD+
-
-
-
?
diacetyl + NADH + H+
(S)-acetoin + NAD+
-
-
-
r
diacetyl + NADH + H+
(S)-acetoin + NAD+
-
-
-
?
diacetyl + NADH + H+
(S)-acetoin + NAD+
-
-
-
?
diacetyl + NADH + H+
(S)-acetoin + NAD+
-
-
-
r
diacetyl + NADH + H+
(S)-acetoin + NAD+
-
-
-
?
diacetyl + NADH + H+
(S)-acetoin + NAD+
-
-
-
-
r
diacetyl + NADH + H+
(S)-acetoin + NAD+
-
-
-
?
additional information
?
-
-
the enzyme shows an S-enantioselectivity in the reversible reduction of acetoin so it might be responsible of the meso-butenediol formation from R-acetoin. It acts on racemic acetoin and (S)-acetoin to form (2S,3S)-butane-2,3-diol, EC 1.1.1.76, but also on the (2R,3R)-butane-2,3-diol isomer in the reverse reaction, EC 1.1.1.4
-
-
?
additional information
?
-
-
the enzyme shows an S-enantioselectivity in the reversible reduction of acetoin so it might be responsible of the meso-butenediol formation from R-acetoin. It acts on racemic acetoin and (S)-acetoin to form (2S,3S)-butane-2,3-diol, EC 1.1.1.76, but also on the (2R,3R)-butane-2,3-diol isomer in the reverse reaction, EC 1.1.1.4
-
-
?
additional information
?
-
KC505218
the enzyme also catalyzes the stereospcific reaction of (S)-acetoin reduction to butanediol, EC 1.1.1.76
-
-
?
additional information
?
-
-
the enzyme also catalyzes the stereospcific reaction of (S)-acetoin reduction to butanediol, EC 1.1.1.76
-
-
?
additional information
?
-
KC505218
the enzyme also catalyzes the stereospcific reaction of (S)-acetoin reduction to butanediol, EC 1.1.1.76
-
-
?
additional information
?
-
-
the enzyme also catalyzes the stereospcific reaction of (S)-acetoin reduction to butanediol, EC 1.1.1.76
-
-
?
additional information
?
-
-
Rhodococcus erythropolis WZ010 is capable of producing optically pure (2S,3S)-2,3-butanediol in alcoholic fermentation.
-
-
?
additional information
?
-
Rhodococcus erythropolis WZ010 is capable of producing optically pure (2S,3S)-2,3-butanediol in alcoholic fermentation.
-
-
?
additional information
?
-
-
Rhodococcus erythropolis WZ010 is capable of producing optically pure (2S,3S)-2,3-butanediol in alcoholic fermentation.
-
-
?
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2-oxoglutarate
-
noncompetitive
acetoin
-
noncompetitive, product inhibition
acetone
-
competitive for diacetyl, uncompetitive for NADH
Ag+
-
1 mM, 0.5% of initial activity with substrate diacetyl, 0.5% with substrate 2,3-butanediol, respectively
Cu2+
-
1 mM, 0.2% of initial activity with substrate diacetyl, 1% with substrate 2,3-butanediol, respectively
diacetyl
-
substrate inhibition at concentrations above 80-90 mM
EDTA
-
1 mM, 91% of initial activity with substrate diacetyl, 90% with substrate 2,3-butanediol, respectively
ethyl pyruvate
-
substrate inhibition at concentrations above 80-90 mM
Fe2+
inhibits 91.6% at 2 mM
Fe3+
-
1 mM, 2% of initial activity with substrate diacetyl, 3.5% with substrate 2,3-butanediol, respectively
hexane-2,5-dione
-
noncompetitive
Methyl pyruvate
-
substrate inhibition at concentrations above 80-90 mM
NAD+
-
competitive, product inhibition
Pentane-3-one
-
competitive for diacetyl, uncompetitive for NADH
Al3+
-
1 mM, 4% of initial activity with substrate diacetyl, 6% with substrate 2,3-butanediol, respectively
Zn2+
-
1 mM, 75% of initial activity with substrate diacetyl, 80% with substrate 2,3-butanediol, respectively
Zn2+
inhibits 94.6% at 2 mM
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additional information
acetoin is an important platform chemical with a variety of applications in foods, cosmetics, chemical synthesis, and especially in the asymmetric synthesis of optically active pharmaceuticals. It is also a useful breath biomarker for early lung cancer diagnosis. Enhanced production of optical (S)-acetoin is achieved by a recombinant Escherichia coli whole-cell biocatalyst with NADH regeneration. Development of a systematic approach using in situ-NADH regeneration systems and the and diacetyl reductase. 52.9 g/l of (S)-acetoin with an enantiomeric purity of 99.5% and a productivity of 6.2 g/l/h are obtained, production of (S)-acetoin can be effectively improved through the engineering of cofactor regeneration with diacetyl reductase and Gdh or Fdh
additional information
selection of an endogenous 2,3-butanediol pathway in Escherichia coli by fermentative redox balance, overview. Anaerobic growth rescue with feeding of acetoin of the deletion mutant strain JCL166 transformed with the designated plasmid carrying the Kp-BudC, Cb-Adh, or the Ec-GldA. substrate-decoupled selection platform based on anaerobic redox balance
additional information
acetoin is an important platform chemical with a variety of applications in foods, cosmetics, chemical synthesis, and especially in the asymmetric synthesis of optically active pharmaceuticals. It is also a useful breath biomarker for early lung cancer diagnosis. Enhanced production of optical (S)-acetoin is achieved by a recombinant Escherichia coli whole-cell biocatalyst with NADH regeneration. Development of a systematic approach using in situ-NADH regeneration systems and the and diacetyl reductase. 52.9 g/l of (S)-acetoin with an enantiomeric purity of 99.5% and a productivity of 6.2 g/l/h are obtained, production of (S)-acetoin can be effectively improved through the engineering of cofactor regeneration with diacetyl reductase and Gdh or Fdh
additional information
acetoin is an important platform chemical with a variety of applications in foods, cosmetics, chemical synthesis, and especially in the asymmetric synthesis of optically active pharmaceuticals. It is also a useful breath biomarker for early lung cancer diagnosis. Enhanced production of optical (S)-acetoin is achieved by a recombinant Escherichia coli whole-cell biocatalyst with NADH regeneration. Development of a systematic approach using in situ-NADH regeneration systems and diacetyl reductase. 52.9 g/l of (S)-acetoin with an enantiomeric purity of 99.5% and a productivity of 6.2 g/l/h are obtained, production of (S)-acetoin can be effectively improved through the engineering of cofactor regeneration with diacetyl reductase and Gdh or Fdh
additional information
acetoin is an important platform chemical with a variety of applications in foods, cosmetics, chemical synthesis, and especially in the asymmetric synthesis of optically active pharmaceuticals. It is also a useful breath biomarker for early lung cancer diagnosis. Enhanced production of optical (S)-acetoin is achieved by a recombinant Escherichia coli whole-cell biocatalyst with NADH regeneration. Development of a systematic approach using in situ-NADH regeneration systems and the and diacetyl reductase. 52.9 g/l of (S)-acetoin with an enantiomeric purity of 99.5% and a productivity of 6.2 g/l/h are obtained, production of (S)-acetoin can be effectively improved through the engineering of cofactor regeneration with diacetyl reductase and Gdh or Fdh
additional information
-
acetoin is an important platform chemical with a variety of applications in foods, cosmetics, chemical synthesis, and especially in the asymmetric synthesis of optically active pharmaceuticals. It is also a useful breath biomarker for early lung cancer diagnosis. Enhanced production of optical (S)-acetoin is achieved by a recombinant Escherichia coli whole-cell biocatalyst with NADH regeneration. Development of a systematic approach using in situ-NADH regeneration systems and the and diacetyl reductase. 52.9 g/l of (S)-acetoin with an enantiomeric purity of 99.5% and a productivity of 6.2 g/l/h are obtained, production of (S)-acetoin can be effectively improved through the engineering of cofactor regeneration with diacetyl reductase and Gdh or Fdh
-
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expression in Escherichia coli
gene adr, DNA and amino acid sequence determination and analysis, sequence comparison
gene adr, DNA and amino acid sequence determination and analysis, sequence comparison, expression of His-tagged enzyme in Escherichia coli
gene budC, functional recombinant expression of NADH-dependent Kp-BudC from plasmid pKM3 in Escherichia coli wild-type strain BW25113 and in mutant strain JCL166 (BW25113/F' [traD36, proABþ, lacIqZ DELTAM15 (Tet)] JCL16 DELTAadhE DELTAldhA DELTAfrdBC)
gene dar, fucntional expression in Escherichia coli strain Rosetta (DE3), resulting in production of S-acetoin with higher than 99.9% optical purity from diacetyl
KC505218
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha, coexpression with formate dehydrogenase (FDH) gene fdh from Saccharomyces cerevisiae
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha, coexpression with formate dehydrogenase (FDH) gene fdh from Saccharomyces cerevisiae or glucose dehydrogenase (GDH) gene gdh from Bacillus subtilis
expression in Escherichia coli
-
expression in Escherichia coli
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha, coexpression with formate dehydrogenase (FDH) gene fdh from Saccharomyces cerevisiae
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha, coexpression with formate dehydrogenase (FDH) gene fdh from Saccharomyces cerevisiae
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha, coexpression with formate dehydrogenase (FDH) gene fdh from Saccharomyces cerevisiae
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synthesis
acetoin(diacetyl) reductase, i.e. 2,3-butanediol dehydrogenase, is one of the key enzymes in the microbial production of 2,3-butanediol, a platform with extensive industrial applications in the production of plastics, printing inks, perfumes, fumigants, spandex, moistening and softening agents, plasticizers, and pharmaceutical carrier
synthesis
KC505218
the enzyme is used for production of S-acetoin with higher than 99.9% optical purity from diacetyl using whole cells of engineered Escherichia coli
synthesis
-
acetoin(diacetyl) reductase, i.e. 2,3-butanediol dehydrogenase, is one of the key enzymes in the microbial production of 2,3-butanediol, a platform with extensive industrial applications in the production of plastics, printing inks, perfumes, fumigants, spandex, moistening and softening agents, plasticizers, and pharmaceutical carrier
-
synthesis
-
the enzyme is used for production of S-acetoin with higher than 99.9% optical purity from diacetyl using whole cells of engineered Escherichia coli
-
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Carballo, J.; Martin, R.; Bernardo, A.; Gonzalez, J.
Purification, characterization and some properties of diacetyl(acetoin) reductase from Enterobacter aerogenes
Eur. J. Biochem.
198
327-332
1991
Klebsiella aerogenes
brenda
Martin, R.; Diez, V.; Burgos, J.
Pigeon liver diacetyl reductase. Effects of pH on the kinetic parameters of the reaction
Biochim. Biophys. Acta
429
293-300
1976
Columba livia
brenda
Burgos, J.; Martin, R.; Diez, V.
Pigeon liver diacetyl reductase. Kinetic and thermodynamic studies with NADH as coenzyme
Biochim. Biophys. Acta
364
9-16
1974
Columba livia
brenda
Vidal, I.; Gonzalez, J.; Bernardo, A.; Martin, R.
Purification and classification of diacetyl-reducing enzymes from Staphylococcus aureus
Biochem. J.
251
461-466
1988
Staphylococcus aureus
brenda
Giovannini, P.P.; Medici, A; Bergamini, C.M.; Rippa, M.
Properties of diacetyl (acetoin) reductase from Bacillus stearothermophilus
Bioorg. Med. Chem.
4
1197-1201
1996
Geobacillus stearothermophilus
brenda
Ui, S.; Okajima, Y.; Mimura, A.; Kanai, H.; kobayashi, T.; Kudo, T.
Sequence analysis of the gene for and characterization of D-acetoin forming meso-2,3-butanediol dehydrogenase of Klebsiella pneumoniae expressed in Escherichia coli
J. Ferment. Bioeng.
83
32-37
1997
Klebsiella pneumoniae (Q48436)
-
brenda
Wang, Z.; Song, Q.; Yu, M.; Wang, Y.; Xiong, B.; Zhang, Y.; Zheng, J.; Ying, X.
Characterization of a stereospecific acetoin(diacetyl) reductase from Rhodococcus erythropolis WZ010 and its application for the synthesis of (2S,3S)-2,3-butanediol
Appl. Microbiol. Biotechnol.
98
641-650
2014
Rhodococcus erythropolis, Rhodococcus erythropolis (C0ZPN9), Rhodococcus erythropolis PR4 (C0ZPN9), Rhodococcus erythropolis WZ010
brenda
Giovannini, P.; Mantovani, M.; Grandini, A.; Medici, A.; Pedrini, P.
New acetoin reductases from Bacillus stearothermophilus: meso- and 2R,3R-butanediol as fermentation products
J. Mol. Catal. B
69
15-20
2011
Geobacillus stearothermophilus, Geobacillus stearothermophilus ATCC 2027
-
brenda
Gao, J.; Xu, Y.; Li, F.; Ding, G.
Production of S-acetoin from diacetyl by Escherichia coli transformant cells that express the diacetyl reductase gene of Paenibacillus polymyxa ZJ-9
Lett. Appl. Microbiol.
57
274-281
2013
Paenibacillus polymyxa (KC505218), Paenibacillus polymyxa, Paenibacillus polymyxa ZJ-9 (KC505218), Paenibacillus polymyxa ZJ-9
brenda
Xu, G.C.; Bian, Y.Q.; Han, R.Z.; Dong, J.J.; Ni, Y.
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