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Literature summary for 1.1.1.6 extracted from

  • Wang, L.; Wang, J.; Shi, H.; Gu, H.; Zhang, Y.; Li, X.; Wang, F.
    Characterization of glycerol dehydrogenase from Thermoanaerobacterium thermosaccharolyticum DSM 571 and GGG motif identification (2016), J. Microbiol. Biotechnol., 26, 1077-1086.
    View publication on PubMed
Search for more literature for 1.1.1.6

Cloned(Commentary)

Cloned (Comment) Organism
gene gldA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Thermoanaerobacterium thermosaccharolyticum

Inhibitors

Inhibitors Comment Organism Structure
Ca2+
-
 Thermoanaerobacterium thermosaccharolyticum
SDS
-
 Thermoanaerobacterium thermosaccharolyticum
Tween 80
-
 Thermoanaerobacterium thermosaccharolyticum
Zn2+ inhibits 24% at 1 mM Thermoanaerobacterium thermosaccharolyticum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.06
-
 NADH pH 6.0, 60°C, recombinant enzyme Thermoanaerobacterium thermosaccharolyticum
1.08
-
 Glycerone pH 6.0, 60°C, recombinant enzyme Thermoanaerobacterium thermosaccharolyticum
30.29
-
 glycerol pH 8.0, 60°C, recombinant enzyme Thermoanaerobacterium thermosaccharolyticum

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ presence of Mn2+ enhances the enzyme activity by 31.4% Thermoanaerobacterium thermosaccharolyticum
Cu2+ presence of Mn2+ enhances the enzyme activity by 37.0% Thermoanaerobacterium thermosaccharolyticum
Mn2+ presence of Mn2+ enhances the enzyme activity by 79.5% Thermoanaerobacterium thermosaccharolyticum
additional information three highly conserved enzyme residues, Asp171, His254, and His271, are associated with metal ion binding Thermoanaerobacterium thermosaccharolyticum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40400
-
-
 Thermoanaerobacterium thermosaccharolyticum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
glycerol + NAD+ Thermoanaerobacterium thermosaccharolyticum
-
 glycerone + NADH + H+
-
 r
glycerol + NAD+ Thermoanaerobacterium thermosaccharolyticum DSM 571
-
 glycerone + NADH + H+
-
 r

Organism

Organism UniProt Comment Textmining
Thermoanaerobacterium thermosaccharolyticum
-
-
-
Thermoanaerobacterium thermosaccharolyticum DSM 571
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Thermoanaerobacterium thermosaccharolyticum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glycerol + NAD+
-
 Thermoanaerobacterium thermosaccharolyticum glycerone + NADH + H+
-
 r
glycerol + NAD+ glycerone reduction is the dominant reaction Thermoanaerobacterium thermosaccharolyticum glycerone + NADH + H+ i.e. 1,3-dihydroxypropranone r
glycerol + NAD+
-
 Thermoanaerobacterium thermosaccharolyticum DSM 571 glycerone + NADH + H+
-
 r
glycerol + NAD+ glycerone reduction is the dominant reaction Thermoanaerobacterium thermosaccharolyticum DSM 571 glycerone + NADH + H+ i.e. 1,3-dihydroxypropranone r
additional information enzyme TtGlyDH preferentially catalyzes 1,3-dihydroxypropranone reduction rather than alcohol compound oxidation. Glycerol oxidization activity is faintly detected in the presence of a high concentration of glycerol (137 mM). No activity is detected with primary alcohols or diols. The highest glycerol oxidation activity is observed at the optimal growth temperature of 60°C in Tris-HCl buffer (50 mM, pH 8.0). Maximum DHA reduction activity is also observed at 60°C, and TtGlyDH exhibits the highest activity in an acetate buffer, compared with 91% maximum activity in an imidazole buffer at the same pH of 6.0 Thermoanaerobacterium thermosaccharolyticum ?
-
 ?
additional information enzyme TtGlyDH preferentially catalyzes 1,3-dihydroxypropranone reduction rather than alcohol compound oxidation. Glycerol oxidization activity is faintly detected in the presence of a high concentration of glycerol (137 mM). No activity is detected with primary alcohols or diols. The highest glycerol oxidation activity is observed at the optimal growth temperature of 60°C in Tris-HCl buffer (50 mM, pH 8.0). Maximum DHA reduction activity is also observed at 60°C, and TtGlyDH exhibits the highest activity in an acetate buffer, compared with 91% maximum activity in an imidazole buffer at the same pH of 6.0 Thermoanaerobacterium thermosaccharolyticum DSM 571 ?
-
 ?

Subunits

Subunits Comment Organism
? x * 40400, recombinant enzyme, SDS-PAGE Thermoanaerobacterium thermosaccharolyticum

Synonyms

Synonyms Comment Organism
GldA
-
 Thermoanaerobacterium thermosaccharolyticum
GlyDH
-
 Thermoanaerobacterium thermosaccharolyticum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
 both reaction directions Thermoanaerobacterium thermosaccharolyticum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
55
-
 recombinant enzyme, maintaining 70% activity after 2 h Thermoanaerobacterium thermosaccharolyticum
60
-
 recombinant enzyme, maintaining 65% activity after 2 h Thermoanaerobacterium thermosaccharolyticum
60 70 recombinant enzyme, maintaining over 80% activity after 30 min Thermoanaerobacterium thermosaccharolyticum
70
-
 recombinant enzyme, maintaining 19% activity after 2 h Thermoanaerobacterium thermosaccharolyticum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.89
-
 glycerol pH 8.0, 60°C, recombinant enzyme Thermoanaerobacterium thermosaccharolyticum
98.44
-
 Glycerone pH 6.0, 60°C, recombinant enzyme Thermoanaerobacterium thermosaccharolyticum

pH Range

pH Minimum pH Maximum Comment Organism
6
-
 glycerone reduction Thermoanaerobacterium thermosaccharolyticum
8
-
 glycerol oxidation Thermoanaerobacterium thermosaccharolyticum

Cofactor

Cofactor Comment Organism Structure
additional information the enzyme's atypical dinucleotide binding motif (GGG motif) and basic residue Arg43 are both related to dinucleotide binding Thermoanaerobacterium thermosaccharolyticum
NAD+
-
 Thermoanaerobacterium thermosaccharolyticum
NADH
-
 Thermoanaerobacterium thermosaccharolyticum

General Information

General Information Comment Organism
evolution 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 Thermoanaerobacterium thermosaccharolyticum
additional information 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 Thermoanaerobacterium thermosaccharolyticum
physiological function glycerol dehydrogenases (GlyDHs) are essential for glycerol metabolism in vivo, catalyzing its reversible reduction to 1,3-dihydroxypropranone Thermoanaerobacterium thermosaccharolyticum

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.06
-
 glycerol pH 8.0, 60°C, recombinant enzyme Thermoanaerobacterium thermosaccharolyticum
91.15
-
 Glycerone pH 6.0, 60°C, recombinant enzyme Thermoanaerobacterium thermosaccharolyticum