ArticleJournal of bacteriology2002
Mycobacterium smegmatis L-alanine dehydrogenase (Ald) is required for proficient utilization of alanine as a sole nitrogen source and sustained anaerobic growth.
Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 50 citations in OpenAlex.
- A Key Metabolic Protein in Active Mycobacterium tuberculosis: Insights into Carbon, Nitrogen, and Sulfur Metabolism.Advances in experimental medicine and biology · 2026Review
- Regulation of the Ald gene encoding alanine dehydrogenase and its induction of ammonium-tolerant nitrogen fixation in Paenibacillus polymyxa WLY78.Microbial cell factories · 2025Article
- Culture-supported ecophysiology of the SAR116 clade demonstrates metabolic and spatial niche partitioning.The ISME journal · 2025Article
- Mycobacterium tuberculosis suppresses host antimicrobial peptides by dehydrogenating L-alanine.Nature communications · 2024Article
- A novel and dual digestive symbiosis scales up the nutrition and immune system of the holobiont Rimicaris exoculata.Microbiome · 2022Article
- Metabolomic changes in Mycobacterium avium subsp. paratuberculosis (MAP) challenged Holstein-Friesian cattle highlight the role of serum amino acids as indicators of immune system activation.Metabolomics : Official journal of the Metabolomic Society · 2022Article
- Function and Characterization of an Alanine Dehydrogenase Homolog FromFrontiers in veterinary science · 2021Article
- Article
- Comparative transcriptomics reveals PrrAB-mediated control of metabolic, respiration, energy-generating, and dormancy pathways in Mycobacterium smegmatis.BMC genomics · 2019Article
- Alanine dehydrogenases in mycobacteria.Journal of microbiology (Seoul, Korea) · 2019Review
- A New Antisense Phosphoryl Guanidine Oligo-2'-O-Methylribonucleotide Penetrates Into Intracellular Mycobacteria and Suppresses Target Gene Expression.Frontiers in pharmacology · 2019Article
- Roles of Alanine Dehydrogenase and Induction of Its Gene in Mycobacterium smegmatis under Respiration-Inhibitory Conditions.Journal of bacteriology · 2018Article
- Assessment of Metabolic Changes in Mycobacterium smegmatis Wild-Type and alr Mutant Strains: Evidence of a New Pathway of d-Alanine Biosynthesis.Journal of proteome research · 2017Article
- Role of Alanine Dehydrogenase of Mycobacterium tuberculosis during Recovery from Hypoxic Nonreplicating Persistence.PloS one · 2016Article
- Regulation Mechanism of the ald Gene Encoding Alanine Dehydrogenase in Mycobacterium smegmatis and Mycobacterium tuberculosis by the Lrp/AsnC Family Regulator AldR.Journal of bacteriology · 2015Article
- Alteration of substrate specificity of alanine dehydrogenase.Protein engineering, design & selection : PEDS · 2015Article
- Generation and screening of a comprehensive Mycobacterium avium subsp. paratuberculosis transposon mutant bank.Frontiers in cellular and infection microbiology · 2014Article
- Salicylanilide diethyl phosphates as potential inhibitors of some mycobacterial enzymes.TheScientificWorldJournal · 2014Article
- Regulation of the ald gene encoding alanine dehydrogenase by AldR in Mycobacterium smegmatis.Journal of bacteriology · 2013Article
- AdeR, a PucR-type transcription factor, activates expression of L-alanine dehydrogenase and is required for sporulation of Bacillus subtilis.Journal of bacteriology · 2012Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
NAD(H)-dependent L-alanine dehydrogenase (EC 1.4.1.1) (Ald) catalyzes the oxidative deamination of L-alanine and the reductive amination of pyruvate. To assess the physiological role of Ald in Mycobacterium smegmatis, we cloned the ald gene, identified its promoter, determined the protein expression levels, and analyzed the combined effects of nutrient supplementation, oxygen availability, and growth stage on enzyme activity. High Ald activities were observed in cells grown in the presence of L- or D-alanine regardless of the oxygen availability and growth stage. In exponentially growing cells under aerobic conditions, supplementation with alanine resulted in a 25- to 50-fold increase in the enzyme activity. In the absence of alanine supplementation, 23-fold-higher Ald activities were observed in cells grown exponentially under anaerobic conditions. Furthermore, M. smegmatis ald null mutants were constructed by targeted disruption and were shown to lack any detectable Ald activity. In contrast, the glycine dehydrogenase (EC 1.4.1.10) (Gdh) activity in mutant cells remained at wild-type levels, indicating that another enzyme protein is responsible for the physiologically relevant reductive amination of glyoxylate. The ald mutants grew poorly in minimal medium with L-alanine as the sole nitrogen source, reaching a saturation density 100-fold less than that of the wild-type strain. Likewise, mutants grew to a saturation density 10-fold less than that of the wild-type strain under anaerobic conditions. In summary, the phenotypes displayed by the M. smegmatis ald mutants suggest that Ald plays an important role in both alanine utilization and anaerobic growth.
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