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evolution
the (2R,3R)-2,3-butanediol dehydrogenase belongs to the mostly zinc-containing medium-chain dehydrogenase/reductase superfamily and not to the short-chain dehydrogenase/reductase superfamily, to which meso- and (2S,3S)-2,3-butanediol dehydrogenases belong, phylogenetic analysis. The enzyme contains two hydrophobic residues forming the binding site for cofactor NAD(P), Phe138 and Leu141 (numbers refer to R,R-BDH of Saccharomyces cerevisiae)
evolution
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the enzyme has homology to the medium-chain dehydrogenases/reductases with preference for secondary alcohols, phylogenetic analysis
evolution
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the enzyme has homology to the medium-chain dehydrogenases/reductases with preference for secondary alcohols, phylogenetic analysis
evolution
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the enzyme has homology to the medium-chain dehydrogenases/reductases with preference for secondary alcohols, phylogenetic analysis
evolution
the enzyme has homology to the medium-chain dehydrogenases/reductases with preference for secondary alcohols, phylogenetic analysis
evolution
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the Serratia marcescens enzyme belongs to the type III Fe-ADH superfamily, three consecutive glycine residues belong to a 14-amino acid residue motif (GDK motif) as the coenzyme NAD(H) binding site, and three conserved histidine residues belong to a 16-residue segment that is homologous to the 15-residue stretch as the binding site of metal
evolution
enzyme BtBDH contains a GroES-like domain at the N terminus and a NAD(P)-binding domain at the C-terminus. Phylogenetic tree analysis reveals that BtBDH is a member ofthe (2R,3R)-2,3-BDH group. BtBDH has the typical (2R,3R)-2,3-butanediol dehydrogenase properties and belongs to the MDR superfamily. According to previous reports, (2R,3R)-2,3-BDH generally belongs to the MDR family, while meso-2,3-BDH is commonly clustered in the SDR (short chain dehydrogenase/reductase) family
evolution
the R-selective 2,3-butanediol dehydrogenase from Bacillus clausii strain DSM 8716 (BcBDH) belongs to the metal-dependent medium chain dehydrogenases/reductases family (MDR)
evolution
two (2R,3R)-2,3-butanediol dehydrogenases (BDHs) from industrial (denoted Y)/laboratory (denoted B) strains of Saccharomyces cerevisiae, Bdh1p(Y)/Bdh1p(B) and Bdh2p(Y)/Bdh2p(B), are members of the PDH subfamily with an NAD(P)H binding domain and a catalytic zinc binding domain, and exhibit reductive activities towards lignocellulosic aldehyde inhibitors, such as acetaldehyde, glycolaldehyde, and furfural
evolution
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the Serratia marcescens enzyme belongs to the type III Fe-ADH superfamily, three consecutive glycine residues belong to a 14-amino acid residue motif (GDK motif) as the coenzyme NAD(H) binding site, and three conserved histidine residues belong to a 16-residue segment that is homologous to the 15-residue stretch as the binding site of metal
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evolution
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two (2R,3R)-2,3-butanediol dehydrogenases (BDHs) from industrial (denoted Y)/laboratory (denoted B) strains of Saccharomyces cerevisiae, Bdh1p(Y)/Bdh1p(B) and Bdh2p(Y)/Bdh2p(B), are members of the PDH subfamily with an NAD(P)H binding domain and a catalytic zinc binding domain, and exhibit reductive activities towards lignocellulosic aldehyde inhibitors, such as acetaldehyde, glycolaldehyde, and furfural
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evolution
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the R-selective 2,3-butanediol dehydrogenase from Bacillus clausii strain DSM 8716 (BcBDH) belongs to the metal-dependent medium chain dehydrogenases/reductases family (MDR)
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evolution
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enzyme BtBDH contains a GroES-like domain at the N terminus and a NAD(P)-binding domain at the C-terminus. Phylogenetic tree analysis reveals that BtBDH is a member ofthe (2R,3R)-2,3-BDH group. BtBDH has the typical (2R,3R)-2,3-butanediol dehydrogenase properties and belongs to the MDR superfamily. According to previous reports, (2R,3R)-2,3-BDH generally belongs to the MDR family, while meso-2,3-BDH is commonly clustered in the SDR (short chain dehydrogenase/reductase) family
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evolution
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the (2R,3R)-2,3-butanediol dehydrogenase belongs to the mostly zinc-containing medium-chain dehydrogenase/reductase superfamily and not to the short-chain dehydrogenase/reductase superfamily, to which meso- and (2S,3S)-2,3-butanediol dehydrogenases belong, phylogenetic analysis. The enzyme contains two hydrophobic residues forming the binding site for cofactor NAD(P), Phe138 and Leu141 (numbers refer to R,R-BDH of Saccharomyces cerevisiae)
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malfunction
deletion of bdhA gene successfully blocks the reversible transformation between acetoin and 2,3-butanediol and eliminates the effect of dissolved oxygen on the transformation
malfunction
the amount of (2R,3R)-2,3-BD is highly reduced in a DELTAacoR mutant lacking the regulatory protein AcoR. The loss of locus pa4153, encoding (2R,3R)-2,3-BDH, has no effect on the ability of this strain to grow in (2S,3S)-2,3-BD but completely impairs its ability to utilize (2R,3R)-2,3-BD and meso-2,3-BD. The complementation of the pa4153 mutant strain with its gene successfully restores the growth ability. The DELTApa4153 PAO1 strain can grow in racemic acetoin, indicating that (2R,3R)-2,3-BDH contributes to 2,3-BD utilization by converting 2,3-BD into acetoin
malfunction
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the amount of (2R,3R)-2,3-BD is highly reduced in a DELTAacoR mutant lacking the regulatory protein AcoR. The loss of locus pa4153, encoding (2R,3R)-2,3-BDH, has no effect on the ability of this strain to grow in (2S,3S)-2,3-BD but completely impairs its ability to utilize (2R,3R)-2,3-BD and meso-2,3-BD. The complementation of the pa4153 mutant strain with its gene successfully restores the growth ability. The DELTApa4153 PAO1 strain can grow in racemic acetoin, indicating that (2R,3R)-2,3-BDH contributes to 2,3-BD utilization by converting 2,3-BD into acetoin
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malfunction
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the amount of (2R,3R)-2,3-BD is highly reduced in a DELTAacoR mutant lacking the regulatory protein AcoR. The loss of locus pa4153, encoding (2R,3R)-2,3-BDH, has no effect on the ability of this strain to grow in (2S,3S)-2,3-BD but completely impairs its ability to utilize (2R,3R)-2,3-BD and meso-2,3-BD. The complementation of the pa4153 mutant strain with its gene successfully restores the growth ability. The DELTApa4153 PAO1 strain can grow in racemic acetoin, indicating that (2R,3R)-2,3-BDH contributes to 2,3-BD utilization by converting 2,3-BD into acetoin
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malfunction
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the amount of (2R,3R)-2,3-BD is highly reduced in a DELTAacoR mutant lacking the regulatory protein AcoR. The loss of locus pa4153, encoding (2R,3R)-2,3-BDH, has no effect on the ability of this strain to grow in (2S,3S)-2,3-BD but completely impairs its ability to utilize (2R,3R)-2,3-BD and meso-2,3-BD. The complementation of the pa4153 mutant strain with its gene successfully restores the growth ability. The DELTApa4153 PAO1 strain can grow in racemic acetoin, indicating that (2R,3R)-2,3-BDH contributes to 2,3-BD utilization by converting 2,3-BD into acetoin
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malfunction
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the amount of (2R,3R)-2,3-BD is highly reduced in a DELTAacoR mutant lacking the regulatory protein AcoR. The loss of locus pa4153, encoding (2R,3R)-2,3-BDH, has no effect on the ability of this strain to grow in (2S,3S)-2,3-BD but completely impairs its ability to utilize (2R,3R)-2,3-BD and meso-2,3-BD. The complementation of the pa4153 mutant strain with its gene successfully restores the growth ability. The DELTApa4153 PAO1 strain can grow in racemic acetoin, indicating that (2R,3R)-2,3-BDH contributes to 2,3-BD utilization by converting 2,3-BD into acetoin
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malfunction
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the amount of (2R,3R)-2,3-BD is highly reduced in a DELTAacoR mutant lacking the regulatory protein AcoR. The loss of locus pa4153, encoding (2R,3R)-2,3-BDH, has no effect on the ability of this strain to grow in (2S,3S)-2,3-BD but completely impairs its ability to utilize (2R,3R)-2,3-BD and meso-2,3-BD. The complementation of the pa4153 mutant strain with its gene successfully restores the growth ability. The DELTApa4153 PAO1 strain can grow in racemic acetoin, indicating that (2R,3R)-2,3-BDH contributes to 2,3-BD utilization by converting 2,3-BD into acetoin
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malfunction
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the amount of (2R,3R)-2,3-BD is highly reduced in a DELTAacoR mutant lacking the regulatory protein AcoR. The loss of locus pa4153, encoding (2R,3R)-2,3-BDH, has no effect on the ability of this strain to grow in (2S,3S)-2,3-BD but completely impairs its ability to utilize (2R,3R)-2,3-BD and meso-2,3-BD. The complementation of the pa4153 mutant strain with its gene successfully restores the growth ability. The DELTApa4153 PAO1 strain can grow in racemic acetoin, indicating that (2R,3R)-2,3-BDH contributes to 2,3-BD utilization by converting 2,3-BD into acetoin
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malfunction
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deletion of bdhA gene successfully blocks the reversible transformation between acetoin and 2,3-butanediol and eliminates the effect of dissolved oxygen on the transformation
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malfunction
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the amount of (2R,3R)-2,3-BD is highly reduced in a DELTAacoR mutant lacking the regulatory protein AcoR. The loss of locus pa4153, encoding (2R,3R)-2,3-BDH, has no effect on the ability of this strain to grow in (2S,3S)-2,3-BD but completely impairs its ability to utilize (2R,3R)-2,3-BD and meso-2,3-BD. The complementation of the pa4153 mutant strain with its gene successfully restores the growth ability. The DELTApa4153 PAO1 strain can grow in racemic acetoin, indicating that (2R,3R)-2,3-BDH contributes to 2,3-BD utilization by converting 2,3-BD into acetoin
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metabolism
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BDH2 is a gene adjacent to BDH1, and these genes are regulated reciprocally. BDH2 is only responsible for converting diacetyl into acetoin, but not for the metabolic pathway of acetoin to 2,3-butanediol in Saccharomyces uvarum
metabolism
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overview of 2,3-BDL biosynthesis pathway and byproducts in microaerobic conditions of Paenibacillus polymyxa strain DSM 365 starting from sucrose as a substrate
metabolism
the proposed pathway from glucose to 2,3-butanediol in Paenibacillus brasilensis involves the enzyme, overview
metabolism
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overview of 2,3-BDL biosynthesis pathway and byproducts in microaerobic conditions of Paenibacillus polymyxa strain DSM 365 starting from sucrose as a substrate
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metabolism
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BDH2 is a gene adjacent to BDH1, and these genes are regulated reciprocally. BDH2 is only responsible for converting diacetyl into acetoin, but not for the metabolic pathway of acetoin to 2,3-butanediol in Saccharomyces uvarum
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metabolism
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the proposed pathway from glucose to 2,3-butanediol in Paenibacillus brasilensis involves the enzyme, overview
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physiological function
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deletion of BDH1 results in an accumulation of acetoin and a diminution of 2,3-butanediol in two Saccharomyces cerevisiae strains under two different growth conditions
physiological function
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glycerol/1,2-propanediol dehydrogenase GldA is the major enzyme responsible for the acetoin reducing activity observed in Escherichia coli
physiological function
22,3-butanediol (2,3-BD) exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD. All three stereoisomers are transformed into acetoin by (2R,3R)-2,3-butanediol dehydrogenase (BDH) or (2S,3S)-2,3-BDH. Acetoin is cleaved to form acetyl-CoA and acetaldehyde by acetoin dehydrogenase enzyme system (AoDH ES). Genes encoding (2R,3R)-2,3-BDH, (2S,3S)-2,3-BDH and the E1 and E2 components of AoDH ES are identified as part of a 2,3-BD utilization operon. In addition, the regulatory protein AcoR promotes the expression of this operon using acetaldehyde, a cleavage product of acetoin, as its direct effector. Proposed model for 2,3-BD utilization in Pseudomonas aeruginosa strain PAO1 in downstream catabolic pathways, overview. Genes pa4148, pa4149, pa4150, pa4151, pa4152 and pa4153 comprise an operon responsible for 2,3-BD utilization, mutational analysis. Acetaldehyde is the direct inducer of the 2,3-BD utilization operon
physiological function
acetoin and 2,3-butanediol can be transformed into each other by 2,3-butanediol dehydrogenase (BDH) using NADH/NAD+ as coenzyme. The main 2,3-butanediol production of strain BS168D is meso-2,3-butanediol and the bdhA gene is only responsible for (2R,3R)-2,3-butanediol synthesis. Oxygen supply in the culture of Bacillus subtilis has an important impact on the product yield, productivity and 2,3-butanediol formation in acetoin fermentation. In general, high oxygen supply favours acetoin formation and decrease 2,3-butanediol final yield
physiological function
Paenibacillus brasilensis produces 2,3-butanediol (2,3-BDO). And although the gene encoding (S,S)-2,3-butanediol dehydrogenase (EC 1.1.1.76) is found in the genome of Paenibacillus brasilensis strain PB24, only R,R-2,3-butanediol ((R,R)-2,3-butanediol dehydrogenase, EC 1.1.1.4) and meso-2,3-butanediol are detected by gas chromatography under the growth conditions tested. The enzyme is multifunctional as R,R-2,3-butanediol dehydrogenase/meso-2,3-butanediol dehydrogenase/diacetyl reductase
physiological function
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the enzyme is involved in formation of diacetyl in wine
physiological function
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22,3-butanediol (2,3-BD) exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD. All three stereoisomers are transformed into acetoin by (2R,3R)-2,3-butanediol dehydrogenase (BDH) or (2S,3S)-2,3-BDH. Acetoin is cleaved to form acetyl-CoA and acetaldehyde by acetoin dehydrogenase enzyme system (AoDH ES). Genes encoding (2R,3R)-2,3-BDH, (2S,3S)-2,3-BDH and the E1 and E2 components of AoDH ES are identified as part of a 2,3-BD utilization operon. In addition, the regulatory protein AcoR promotes the expression of this operon using acetaldehyde, a cleavage product of acetoin, as its direct effector. Proposed model for 2,3-BD utilization in Pseudomonas aeruginosa strain PAO1 in downstream catabolic pathways, overview. Genes pa4148, pa4149, pa4150, pa4151, pa4152 and pa4153 comprise an operon responsible for 2,3-BD utilization, mutational analysis. Acetaldehyde is the direct inducer of the 2,3-BD utilization operon
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physiological function
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22,3-butanediol (2,3-BD) exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD. All three stereoisomers are transformed into acetoin by (2R,3R)-2,3-butanediol dehydrogenase (BDH) or (2S,3S)-2,3-BDH. Acetoin is cleaved to form acetyl-CoA and acetaldehyde by acetoin dehydrogenase enzyme system (AoDH ES). Genes encoding (2R,3R)-2,3-BDH, (2S,3S)-2,3-BDH and the E1 and E2 components of AoDH ES are identified as part of a 2,3-BD utilization operon. In addition, the regulatory protein AcoR promotes the expression of this operon using acetaldehyde, a cleavage product of acetoin, as its direct effector. Proposed model for 2,3-BD utilization in Pseudomonas aeruginosa strain PAO1 in downstream catabolic pathways, overview. Genes pa4148, pa4149, pa4150, pa4151, pa4152 and pa4153 comprise an operon responsible for 2,3-BD utilization, mutational analysis. Acetaldehyde is the direct inducer of the 2,3-BD utilization operon
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physiological function
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22,3-butanediol (2,3-BD) exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD. All three stereoisomers are transformed into acetoin by (2R,3R)-2,3-butanediol dehydrogenase (BDH) or (2S,3S)-2,3-BDH. Acetoin is cleaved to form acetyl-CoA and acetaldehyde by acetoin dehydrogenase enzyme system (AoDH ES). Genes encoding (2R,3R)-2,3-BDH, (2S,3S)-2,3-BDH and the E1 and E2 components of AoDH ES are identified as part of a 2,3-BD utilization operon. In addition, the regulatory protein AcoR promotes the expression of this operon using acetaldehyde, a cleavage product of acetoin, as its direct effector. Proposed model for 2,3-BD utilization in Pseudomonas aeruginosa strain PAO1 in downstream catabolic pathways, overview. Genes pa4148, pa4149, pa4150, pa4151, pa4152 and pa4153 comprise an operon responsible for 2,3-BD utilization, mutational analysis. Acetaldehyde is the direct inducer of the 2,3-BD utilization operon
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physiological function
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the enzyme is involved in formation of diacetyl in wine
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physiological function
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22,3-butanediol (2,3-BD) exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD. All three stereoisomers are transformed into acetoin by (2R,3R)-2,3-butanediol dehydrogenase (BDH) or (2S,3S)-2,3-BDH. Acetoin is cleaved to form acetyl-CoA and acetaldehyde by acetoin dehydrogenase enzyme system (AoDH ES). Genes encoding (2R,3R)-2,3-BDH, (2S,3S)-2,3-BDH and the E1 and E2 components of AoDH ES are identified as part of a 2,3-BD utilization operon. In addition, the regulatory protein AcoR promotes the expression of this operon using acetaldehyde, a cleavage product of acetoin, as its direct effector. Proposed model for 2,3-BD utilization in Pseudomonas aeruginosa strain PAO1 in downstream catabolic pathways, overview. Genes pa4148, pa4149, pa4150, pa4151, pa4152 and pa4153 comprise an operon responsible for 2,3-BD utilization, mutational analysis. Acetaldehyde is the direct inducer of the 2,3-BD utilization operon
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physiological function
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glycerol/1,2-propanediol dehydrogenase GldA is the major enzyme responsible for the acetoin reducing activity observed in Escherichia coli
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physiological function
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22,3-butanediol (2,3-BD) exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD. All three stereoisomers are transformed into acetoin by (2R,3R)-2,3-butanediol dehydrogenase (BDH) or (2S,3S)-2,3-BDH. Acetoin is cleaved to form acetyl-CoA and acetaldehyde by acetoin dehydrogenase enzyme system (AoDH ES). Genes encoding (2R,3R)-2,3-BDH, (2S,3S)-2,3-BDH and the E1 and E2 components of AoDH ES are identified as part of a 2,3-BD utilization operon. In addition, the regulatory protein AcoR promotes the expression of this operon using acetaldehyde, a cleavage product of acetoin, as its direct effector. Proposed model for 2,3-BD utilization in Pseudomonas aeruginosa strain PAO1 in downstream catabolic pathways, overview. Genes pa4148, pa4149, pa4150, pa4151, pa4152 and pa4153 comprise an operon responsible for 2,3-BD utilization, mutational analysis. Acetaldehyde is the direct inducer of the 2,3-BD utilization operon
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physiological function
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22,3-butanediol (2,3-BD) exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD. All three stereoisomers are transformed into acetoin by (2R,3R)-2,3-butanediol dehydrogenase (BDH) or (2S,3S)-2,3-BDH. Acetoin is cleaved to form acetyl-CoA and acetaldehyde by acetoin dehydrogenase enzyme system (AoDH ES). Genes encoding (2R,3R)-2,3-BDH, (2S,3S)-2,3-BDH and the E1 and E2 components of AoDH ES are identified as part of a 2,3-BD utilization operon. In addition, the regulatory protein AcoR promotes the expression of this operon using acetaldehyde, a cleavage product of acetoin, as its direct effector. Proposed model for 2,3-BD utilization in Pseudomonas aeruginosa strain PAO1 in downstream catabolic pathways, overview. Genes pa4148, pa4149, pa4150, pa4151, pa4152 and pa4153 comprise an operon responsible for 2,3-BD utilization, mutational analysis. Acetaldehyde is the direct inducer of the 2,3-BD utilization operon
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physiological function
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Paenibacillus brasilensis produces 2,3-butanediol (2,3-BDO). And although the gene encoding (S,S)-2,3-butanediol dehydrogenase (EC 1.1.1.76) is found in the genome of Paenibacillus brasilensis strain PB24, only R,R-2,3-butanediol ((R,R)-2,3-butanediol dehydrogenase, EC 1.1.1.4) and meso-2,3-butanediol are detected by gas chromatography under the growth conditions tested. The enzyme is multifunctional as R,R-2,3-butanediol dehydrogenase/meso-2,3-butanediol dehydrogenase/diacetyl reductase
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physiological function
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acetoin and 2,3-butanediol can be transformed into each other by 2,3-butanediol dehydrogenase (BDH) using NADH/NAD+ as coenzyme. The main 2,3-butanediol production of strain BS168D is meso-2,3-butanediol and the bdhA gene is only responsible for (2R,3R)-2,3-butanediol synthesis. Oxygen supply in the culture of Bacillus subtilis has an important impact on the product yield, productivity and 2,3-butanediol formation in acetoin fermentation. In general, high oxygen supply favours acetoin formation and decrease 2,3-butanediol final yield
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physiological function
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22,3-butanediol (2,3-BD) exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD. All three stereoisomers are transformed into acetoin by (2R,3R)-2,3-butanediol dehydrogenase (BDH) or (2S,3S)-2,3-BDH. Acetoin is cleaved to form acetyl-CoA and acetaldehyde by acetoin dehydrogenase enzyme system (AoDH ES). Genes encoding (2R,3R)-2,3-BDH, (2S,3S)-2,3-BDH and the E1 and E2 components of AoDH ES are identified as part of a 2,3-BD utilization operon. In addition, the regulatory protein AcoR promotes the expression of this operon using acetaldehyde, a cleavage product of acetoin, as its direct effector. Proposed model for 2,3-BD utilization in Pseudomonas aeruginosa strain PAO1 in downstream catabolic pathways, overview. Genes pa4148, pa4149, pa4150, pa4151, pa4152 and pa4153 comprise an operon responsible for 2,3-BD utilization, mutational analysis. Acetaldehyde is the direct inducer of the 2,3-BD utilization operon
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