EC Number   |
General Information |
Reference |
|---|
    1.4.1.1 | evolution |
distribution of Alds in mycobacteria, phylogenetic analysis and tree, overview. Alds of slow-growing mycobacteria are mostly distinct from those of fast-growing mycobacteria |
763354 |
| 1.4.1.1 | evolution |
distribution of Alds in mycobacteria, phylogenetic analysis and tree, overview. Alds of slow-growing mycobacteria are mostly distinct from those of fast-growing mycobacteria. Structure of Ald and phylogenetic relevance of mycobacterial Alds |
-, 763354 |
| 1.4.1.1 | evolution |
sequence comparisons and phylogenetic analysis |
763144 |
| 1.4.1.1 | evolution |
sequence comparisons and phylogenetic analysis indicate that enzyme HAADH1 is a distinct type of alanine dehydrogenase |
763144 |
| 1.4.1.1 | malfunction |
an ald knockout strain grows without alanine or glycine and is able to utilize glycine but not alanine as a nitrogen source |
-, 725267 |
| 1.4.1.1 | malfunction |
an ald mutant of Mycolicibacterium smegmatis is much more sensitive to the bcc1 complex inhibitor Q203 than the isogenic wild-type strain. Another ald mutant of Mycolicibacterium smegmatis reportedly displays decreased survival under oxygen depletion conditions compared with the wild-type strain. When Mycolicibacterium smegmatis strains are treated with KCN under aerobic conditions, expression of the ald gene in a bd quinol oxidase mutant strain of Mycolicibacterium smegmatis expressing only the aa3 cytochrome c oxidase as a terminal oxidase is more induced than that in the corresponding wild-type strain expressing both terminal oxidases. Reduced functionality of the ETC, rather than direct regulation of ald by an O2-sensing regulatory system, is most relevant to hypoxic induction of ald expression |
-, 763354 |
| 1.4.1.1 | malfunction |
growth of Streptomyces coelicolor A3(2) is impacted by the deletion of the alanine dehydrogenase (ALD), an essential enzyme that plays a central role in the carbon and nitrogen metabolism. A long lagphase growth followed by a slow exponential growth of Streptomyces coelicolor due to ALD gene deletion is observed in liquid yeast extract mineral salt culture. The slow lag-phase growth is replaced by the normal wild-type like growth by ALD complementation engineering. Deletion mutant SCDELTAALD spores have a paler appearance compared to the standard brownish gray pigmentation for the wild-type SCWT spores. This reduced pigmentation is complemented, and the standard brownish gray pigmentation reappeares during SC-ALD sporulation |
-, 763371 |
| 1.4.1.1 | malfunction |
mutations at four conserved residue Arg15, Lys75, His-6, and Asp269 (except residue Lys73) result in a complete loss in enzymatic activity, which signifies that these predicted active sites are indispensable for OF4Ald activity |
-, 762981 |
| 1.4.1.1 | malfunction |
the inactivation of ald in Mycobacterium tuberculosis confers a low level of DCS resistance. The mechanism underlying DCS resistance resulting from ald inactivation is suggested as follows: Mycobacterium tuberculosis strains lacking the functional Ald cannot convert L-alanine to pyruvate, resulting in an increase in cellular levels of L-alanine. As DCS is a competitive inhibitor of alanine racemase, inhibition of alanine racemase by DCS might be overcome by increased concentrations of L-alanine that is a substrate of alanine racemase |
-, 763354 |
| 1.4.1.1 | malfunction |
the inhibition of electron flux through the respiratory electron transport chain (ETC) by either the disruption of the gene for the major terminal oxidase (aa3 cytochrome c oxidase) or treatment with KCN results in the induction of ald encoding alanine dehydrogenase in Mycolicibacterium smegmatis. A decrease in functionality of the ETC shifts the redox state of the NADH/NAD+x02pool toward a more reduced state, which in turn leads to an increase in cellular levels of alanine by Ald catalyzing the conversion of pyruvate to alanine with the concomitant oxidation of NADH to NAD+. The induction of ald expression under respiration-inhibitory conditions in Mycolicibacterium smegmatis is mediated by the alanine-responsive AldR transcriptional regulator. The growth defect of the bacteria by respiration inhibition is exacerbated by inactivation of the ald gene |
-, 763206 |
