EC Number   |
General Information |
Reference |
|---|
    1.1.1.6 | evolution |
NAD+-linked GDHs are members of the medium-chain alcohol dehydrogenase family, most of which are metalloenzymes |
741311 |
| 1.1.1.6 | 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 |
-, 740856 |
| 1.1.1.6 | evolution |
the enzyme belongs to the medium-chain dehydrogenase/reductase, MDRase, superfamily |
723679 |
| 1.1.1.6 | evolution |
the NAD+-linked GDHs are members of the medium-chain alcohol dehydrogenase family, most of which are metalloenzymes |
741311 |
| 1.1.1.6 | evolution |
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 |
-, 740827 |
| 1.1.1.6 | 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 |
748573 |
| 1.1.1.6 | metabolism |
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 |
-, 739908 |
| 1.1.1.6 | metabolism |
in Escherichia coli, the enzyme catalyzes the first step in fermentative glycerol metabolism to produce dihydroxyacetone, biochemical transformation pathway of glycerol, overview |
723679 |
| 1.1.1.6 | 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 |
760880 |
| 1.1.1.6 | metabolism |
the enzyme is required to catalyze the first step in fermentative glycerol metabolism |
-, 760298 |
