EC Number |
General Information |
Reference |
---|
1.2.1.10 | evolution |
distribution of ADHE among the five eukaryotic supergroups, overview |
763253 |
1.2.1.10 | evolution |
the bifunctional AdhE enzyme is conserved in all bacterial kingdoms but also in more phylogenetically distant microorganisms such as green microalgae |
763497 |
1.2.1.10 | malfunction |
cells with increased ADHE abundance exhibit better survival under dark anoxia |
763253 |
1.2.1.10 | metabolism |
ADHE can be involved either in ethanol production or assimilation, or both, depending upon environmental conditions. Presence of ADHE in an oxygen-respiring algal mitochondrion and co-expression at ambient oxygen levels with respiratory chain components is unexpected with respect to the view that eukaryotes acquire ADHE genes specifically as an adaptation to an anaerobic lifestyle |
739328 |
1.2.1.10 | 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 |
1.2.1.10 | metabolism |
analysis of the anerobic metabolic routes involving the enzyme in Chlamydomonas reinhardtii, overview |
763253 |
1.2.1.10 | metabolism |
DmpFG catalyzes the final two steps of the meta-cleavage pathway of catechol and its methylated substituents. This pathway breaks down toxic waste products such as naphthalenes, salicylates, and benzoates to harmless metabolites |
-, 727173 |
1.2.1.10 | metabolism |
the oxygen sensitivity of CoA-acylating aldehyde dehydrogenase appears to be a key limiting factor for cyanobacteria to produce alcohols through the CoA-dependent route |
742372 |
1.2.1.10 | more |
filamentation of the bacterial bifunctional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation. Incubation with NAD+ and Fe2+ is sufficient to extend the filaments. The addition of coenzyme A does not impair the conformational change triggered by NAD+ and Fe2+. In the same conditions, NADH and Fe2+ are not able to trigger a conformational change from the compact to the extended form. Comparison of the structure of AdhE in its extended conformation with monofunctional ADH and AlDH enzymes, overview. The substrate/product channels of both the AlDH and ADH domains lead to the two cavities located at the AlDH-ADH interfaces within the AdhE dimer. The loops 2 and 3 seal this cavity by mediating the interactions between the AlDH and ADH domains. This allows a direct channeling between the AlDH and ADH domain active sites |
763497 |
1.2.1.10 | more |
the enzyme's two functional domains are fused into a single polypeptide by a linker amino acid region |
742936 |