1.1.1.6: glycerol dehydrogenase
This is an abbreviated version!
For detailed information about glycerol dehydrogenase, go to the full flat file.
Reaction
Synonyms
B4100_2156, CglD, dehydrogenase, glycerol, GDH, GDH2, GLD, Gld3, GldA, GLDH
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General Information
General Information on EC 1.1.1.6 - glycerol dehydrogenase
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evolution
metabolism
physiological function
additional information
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the enzyme belongs to the medium-chain dehydrogenase/reductase, MDRase, superfamily
evolution
NAD+-linked GDHs are members of the medium-chain alcohol dehydrogenase family, most of which are metalloenzymes
evolution
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the enzyme belongs to the Fe-ADH family. The GXGXXG motif is not present in TtGlyDH or other members of the Fe-ADH family, the GGG motif forms a more flexible turn and provides enough space to accommodate the pyrophosphate moiety of dinucleotides
evolution
the NAD+-linked GDHs are members of the medium-chain alcohol dehydrogenase family, most of which are metalloenzymes
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
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the enzyme belongs to the Fe-ADH family. The GXGXXG motif is not present in TtGlyDH or other members of the Fe-ADH family, the GGG motif forms a more flexible turn and provides enough space to accommodate the pyrophosphate moiety of dinucleotides
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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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in Escherichia coli, the enzyme catalyzes the first step in fermentative glycerol metabolism to produce dihydroxyacetone, biochemical transformation pathway of glycerol, overview
metabolism
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glycerol is one of the key metabolites for propionic acid synthesis in Propionibacterium jensenii. It is a precursor for metabolic pathways for propionic acid, lactic acid, and acetic acid biosynthesis in Propionibacterium
metabolism
anaerobic fermentative metabolism of glycerol: proteome analysis as well as enzyme assays performed in cell-free extracts demonstrate that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen
metabolism
reaction mechanism leads to a proton transfer between the substrate and the acid residue before the hydride transfer from glycerol to NAD+. The mechanism takes place in a stepwise manner, consisting in the proton abstraction of the alcohol by D123 residue followed by the hydride transfer from glycerol to NAD+. This second step is the rate-limiting one
metabolism
the enzyme is required to catalyze the first step in fermentative glycerol metabolism
metabolism
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the native glycerol dehydrogenase in Escherichia coli is identified as the main responsible enzyme for catechol generation
metabolism
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glycerol is one of the key metabolites for propionic acid synthesis in Propionibacterium jensenii. It is a precursor for metabolic pathways for propionic acid, lactic acid, and acetic acid biosynthesis in Propionibacterium
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metabolism
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the native glycerol dehydrogenase in Escherichia coli is identified as the main responsible enzyme for catechol generation
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metabolism
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the enzyme is required to catalyze the first step in fermentative glycerol metabolism
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GroDHase is mainly involved in Gro utilization as a carbon and energy source
physiological function
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glycerol dehydrogenase is the enzyme responsible for the oxidation of glycerol to dihydroxyacetone. This permits its entrance into the glycolytic pathway
physiological function
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glycerol dehydrogenases (GlyDHs) are essential for glycerol metabolism in vivo, catalyzing its reversible reduction to 1,3-dihydroxypropranone
physiological function
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an isoform Gld3 deletion strain has no visible growth defects compared with the control wild-type strain. Disruption of Gld3 leads to the inhibition of kojic acid production, and the expression of KojA, KojR is downregulated in the Gld3 disruption strain. When KojA or KojR is overexpressed in the Gd3 disruption strain, the yield of kojic acid is restored
physiological function
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glycerol dehydrogenases (GlyDHs) are essential for glycerol metabolism in vivo, catalyzing its reversible reduction to 1,3-dihydroxypropranone
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mechanistic study of manganese-substituted glycerol dehydrogenase using a kinetic and thermodynamic analysis, overview. The binding energy of enzyme ternary complex for Mn-GDH and GDH derived from kinetic parameters indicates that metal ion substitution accelerates the release of dioxyacetone. The metal ion plays a role in catalysis enhancement
additional information
mechanistic study of manganese-substituted glycerol dehydrogenase using a kinetic and thermodynamic analysis, overview. The binding energy of enzyme ternary complex for Mn-GDH and GDH derived from kinetic parameters indicates that metal ion substitution accelerates the release of dioxyacetone. The metal ion plays a role in catalysis enhancement
additional information
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molecular modeling and site-directed mutagenesis analyses demonstrate that TtGlyDH has an atypical dinucleotide binding motif (GGG motif) and a basic residue Arg43, both related to dinucleotide binding
additional information
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molecular modeling and site-directed mutagenesis analyses demonstrate that TtGlyDH has an atypical dinucleotide binding motif (GGG motif) and a basic residue Arg43, both related to dinucleotide binding
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