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evolution
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distribution of Alds in mycobacteria, phylogenetic analysis and tree, overview. Alds of slow-growing mycobacteria are mostly distinct from those of fast-growing mycobacteria
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
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
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
evolution
sequence comparisons and phylogenetic analysis
evolution
sequence comparisons and phylogenetic analysis indicate that enzyme HAADH1 is a distinct type of alanine dehydrogenase
evolution
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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
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evolution
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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
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evolution
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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
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evolution
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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
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evolution
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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
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malfunction
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an ald knockout strain grows without alanine or glycine and is able to utilize glycine but not alanine as a nitrogen source
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
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
malfunction
Alkalihalophilus pseudofirmus
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
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
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
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
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malfunction
Alkalihalophilus pseudofirmus OF4
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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
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malfunction
Alkalihalophilus pseudofirmus ATCC BAA-2126
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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
-
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
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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
-
malfunction
Alkalihalophilus pseudofirmus JCM 17055
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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
-
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
-
malfunction
-
an ald knockout strain grows without alanine or glycine and is able to utilize glycine but not alanine as a nitrogen source
-
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
-
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
-
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
-
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
-
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
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metabolism
by catalyzing the NAD+-dependent reversible interconversion of alanine and pyruvate, enzyme ALD plays a central role in the carbon and nitrogen metabolism in all microorganisms. This enzymatic process not only provides alanine as an energy source through the tricarboxylic acid cycle for most bacterial species but it is also the key pathway for de novo alanine synthesis for some microorganisms. The oxidative deamination reaction catalyzed by ALD is required for microorganisms to utilize alanine as a nitrogen source
metabolism
expression of the ald gene is strongly upregulated in Mycolicibacterium smegmatis grown in the presence of alanine. Alanine-dependent regulation of ald is mediated by the AldR transcriptional regulator that belongs to the Lrp/AsnC (leucine-responsive regulatory protein/asparagine synthase C) family
metabolism
regulation mechanism of ald expression by the AldR transcription factor in response to alanine availability, model for the regulation of ald expression by AldR, overview
metabolism
regulation mechanism of ald expression by the AldR transcription factor in response to alanine availability, model for the regulation of ald expression by AldR, overview
metabolism
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regulation mechanism of ald expression by the AldR transcription factor in response to alanine availability, model for the regulation of ald expression by AldR, overview
metabolism
regulation mechanism of ald expression by the AldR transcription factor in response to alanine availability, model for the regulation of ald expression by AldR, overview. AldR exerts its regulatory effect on ald expression by binding AldR binding sites (O1, O2, O3, and O4) bearing a consensus sequence of GA/T-N2-NWW/WWN-N2-T/AC (W = A or T; / = or) in both Mycolicibacterium smegmatis. Three-dimensional structure of AldR and phylogenetic analysis of AldRs from mycobacteria
metabolism
-
by catalyzing the NAD+-dependent reversible interconversion of alanine and pyruvate, enzyme ALD plays a central role in the carbon and nitrogen metabolism in all microorganisms. This enzymatic process not only provides alanine as an energy source through the tricarboxylic acid cycle for most bacterial species but it is also the key pathway for de novo alanine synthesis for some microorganisms. The oxidative deamination reaction catalyzed by ALD is required for microorganisms to utilize alanine as a nitrogen source
-
metabolism
-
regulation mechanism of ald expression by the AldR transcription factor in response to alanine availability, model for the regulation of ald expression by AldR, overview
-
metabolism
-
expression of the ald gene is strongly upregulated in Mycolicibacterium smegmatis grown in the presence of alanine. Alanine-dependent regulation of ald is mediated by the AldR transcriptional regulator that belongs to the Lrp/AsnC (leucine-responsive regulatory protein/asparagine synthase C) family
-
metabolism
-
regulation mechanism of ald expression by the AldR transcription factor in response to alanine availability, model for the regulation of ald expression by AldR, overview. AldR exerts its regulatory effect on ald expression by binding AldR binding sites (O1, O2, O3, and O4) bearing a consensus sequence of GA/T-N2-NWW/WWN-N2-T/AC (W = A or T; / = or) in both Mycolicibacterium smegmatis. Three-dimensional structure of AldR and phylogenetic analysis of AldRs from mycobacteria
-
metabolism
-
by catalyzing the NAD+-dependent reversible interconversion of alanine and pyruvate, enzyme ALD plays a central role in the carbon and nitrogen metabolism in all microorganisms. This enzymatic process not only provides alanine as an energy source through the tricarboxylic acid cycle for most bacterial species but it is also the key pathway for de novo alanine synthesis for some microorganisms. The oxidative deamination reaction catalyzed by ALD is required for microorganisms to utilize alanine as a nitrogen source
-
metabolism
-
regulation mechanism of ald expression by the AldR transcription factor in response to alanine availability, model for the regulation of ald expression by AldR, overview
-
metabolism
-
regulation mechanism of ald expression by the AldR transcription factor in response to alanine availability, model for the regulation of ald expression by AldR, overview
-
metabolism
-
expression of the ald gene is strongly upregulated in Mycolicibacterium smegmatis grown in the presence of alanine. Alanine-dependent regulation of ald is mediated by the AldR transcriptional regulator that belongs to the Lrp/AsnC (leucine-responsive regulatory protein/asparagine synthase C) family
-
metabolism
-
regulation mechanism of ald expression by the AldR transcription factor in response to alanine availability, model for the regulation of ald expression by AldR, overview. AldR exerts its regulatory effect on ald expression by binding AldR binding sites (O1, O2, O3, and O4) bearing a consensus sequence of GA/T-N2-NWW/WWN-N2-T/AC (W = A or T; / = or) in both Mycolicibacterium smegmatis. Three-dimensional structure of AldR and phylogenetic analysis of AldRs from mycobacteria
-
metabolism
-
by catalyzing the NAD+-dependent reversible interconversion of alanine and pyruvate, enzyme ALD plays a central role in the carbon and nitrogen metabolism in all microorganisms. This enzymatic process not only provides alanine as an energy source through the tricarboxylic acid cycle for most bacterial species but it is also the key pathway for de novo alanine synthesis for some microorganisms. The oxidative deamination reaction catalyzed by ALD is required for microorganisms to utilize alanine as a nitrogen source
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physiological function
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the enzyme is involved in the alanine catabolism in the heterocysts, that is needed for normal diazotrophic growth
physiological function
-
enzyme Ald may have several functions, including ammonium incorporation and alanine breakdown. Ald plays an essential role in the utilization of alanine but not of glycine. Ald is not essential for the breakdown of glycine
physiological function
-
the enzyme plays an important role in the carbon and nitrogen metabolism of microorganisms, it iis a key factor in assimilation of L-Ala as energy source through TCA cycle
physiological function
abundance and activity profiles of alanine dehydrogenase concomitantly increase with the onset of enhanced alanine utilization during transition into stationary growth phase
physiological function
both mRNA levels and enzymatic activities of isocitrate lyase, and alanine dehydrogenase increases during entry into nonreplicating persistence. Expression of alanine dehydrogenase is also induced in vitro by persistence-inducing stresses such as nitric oxide, and the gene is expressed at high levels in vivo during the initial lung infection in mice. Enzyme activity is maintained during extended hypoxia even after transcription levels decrease. A knockout mutant shows no reduction in anaerobic survival in vitro, but results in a significant lag in the resumption of growth after reoxygenation. During reactivation the mutant has an altered NADH/NAD ratio
physiological function
AlaDH catalyzes the reversible conversion of L-alanine and pyruvate, which has an important role in the TCA energy cycle
physiological function
Ald is beneficial to Mycolicibacterium smegmatis in its adaptation and survival under respiration-inhibitory conditions by maintaining NADH/NAD+ homeostasis. Ald is required for optimal mycobacterial growth under severe respiration-inhibitory conditions
physiological function
enzyme Ald is implicated in resistance of Mycobacterium tuberculosis to the second-line drug D-cycloserine (DCS). DCS is known to inhibit two enzymes, alanine racemase and D-alanine-D-alanine ligase
physiological function
enzyme Ald is suggested to primarily play a biosynthetic role by catalyzing the reductive amination of pyruvate to alanine as judged by the very small Keq for the oxidative deamination reaction
physiological function
enzyme Ald seems to play a crucial role in the growth and survival of the organism under severe respiration-inhibitory conditions such as the inhibitory condition of both the bcc1-aa3 branch and bd quinol oxidase of the respiratory ETC
physiological function
gene ApalaDH encodes a bifunctional protein catalyzing the reversible reaction of pyruvate to L-alanine via its pyruvate reductive aminase (PvRA) activity, the reaction of L-alanine to pyruvate via its alanine oxidative dehydrogenase activity, and the non-reversible reaction of glyoxylate to glycine via its glyoxylate reductive aminase (GxRA) activity. The assimilatory/dissimilatory roles of enzyme ApAlaDH from the halotolerant cyanobacterium Aphanothece halophytica are not only specific for L-alanine and pyruvate, but also, upon salt stress, include glyoxylate to generate glycine. ApAlaDH is a bifunctional enzyme
physiological function
L-alanine dehydrogenase is a NADH-dependent enzyme that catalyzes the reversible reductive amination of pyruvate using ammonia as amine source
physiological function
-
the enzyme is involved in the alanine catabolism in the heterocysts, that is needed for normal diazotrophic growth
-
physiological function
-
L-alanine dehydrogenase is a NADH-dependent enzyme that catalyzes the reversible reductive amination of pyruvate using ammonia as amine source
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physiological function
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gene ApalaDH encodes a bifunctional protein catalyzing the reversible reaction of pyruvate to L-alanine via its pyruvate reductive aminase (PvRA) activity, the reaction of L-alanine to pyruvate via its alanine oxidative dehydrogenase activity, and the non-reversible reaction of glyoxylate to glycine via its glyoxylate reductive aminase (GxRA) activity. The assimilatory/dissimilatory roles of enzyme ApAlaDH from the halotolerant cyanobacterium Aphanothece halophytica are not only specific for L-alanine and pyruvate, but also, upon salt stress, include glyoxylate to generate glycine. ApAlaDH is a bifunctional enzyme
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physiological function
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Ald is beneficial to Mycolicibacterium smegmatis in its adaptation and survival under respiration-inhibitory conditions by maintaining NADH/NAD+ homeostasis. Ald is required for optimal mycobacterial growth under severe respiration-inhibitory conditions
-
physiological function
-
enzyme Ald seems to play a crucial role in the growth and survival of the organism under severe respiration-inhibitory conditions such as the inhibitory condition of both the bcc1-aa3 branch and bd quinol oxidase of the respiratory ETC
-
physiological function
-
enzyme Ald may have several functions, including ammonium incorporation and alanine breakdown. Ald plays an essential role in the utilization of alanine but not of glycine. Ald is not essential for the breakdown of glycine
-
physiological function
-
both mRNA levels and enzymatic activities of isocitrate lyase, and alanine dehydrogenase increases during entry into nonreplicating persistence. Expression of alanine dehydrogenase is also induced in vitro by persistence-inducing stresses such as nitric oxide, and the gene is expressed at high levels in vivo during the initial lung infection in mice. Enzyme activity is maintained during extended hypoxia even after transcription levels decrease. A knockout mutant shows no reduction in anaerobic survival in vitro, but results in a significant lag in the resumption of growth after reoxygenation. During reactivation the mutant has an altered NADH/NAD ratio
-
physiological function
-
enzyme Ald is implicated in resistance of Mycobacterium tuberculosis to the second-line drug D-cycloserine (DCS). DCS is known to inhibit two enzymes, alanine racemase and D-alanine-D-alanine ligase
-
physiological function
-
enzyme Ald is suggested to primarily play a biosynthetic role by catalyzing the reductive amination of pyruvate to alanine as judged by the very small Keq for the oxidative deamination reaction
-
physiological function
-
enzyme Ald is implicated in resistance of Mycobacterium tuberculosis to the second-line drug D-cycloserine (DCS). DCS is known to inhibit two enzymes, alanine racemase and D-alanine-D-alanine ligase
-
physiological function
-
enzyme Ald is suggested to primarily play a biosynthetic role by catalyzing the reductive amination of pyruvate to alanine as judged by the very small Keq for the oxidative deamination reaction
-
physiological function
-
Ald is beneficial to Mycolicibacterium smegmatis in its adaptation and survival under respiration-inhibitory conditions by maintaining NADH/NAD+ homeostasis. Ald is required for optimal mycobacterial growth under severe respiration-inhibitory conditions
-
physiological function
-
enzyme Ald seems to play a crucial role in the growth and survival of the organism under severe respiration-inhibitory conditions such as the inhibitory condition of both the bcc1-aa3 branch and bd quinol oxidase of the respiratory ETC
-
physiological function
-
abundance and activity profiles of alanine dehydrogenase concomitantly increase with the onset of enhanced alanine utilization during transition into stationary growth phase
-
additional information
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alanine is transported from vegetative cells into heterocysts in the diazotrophic Anabaena filament
additional information
Alkalihalophilus pseudofirmus
five highly conserved amino acid residues Arg15, Lys73, Lys75, His96, and Asp269 are potential catalytic residues of L-alanine dehydrogenase from Bacillus pseudofirmus strain OF4. Enzyme structure homology modeling and structure-function analysis, comparison of the partial potential active site of OF4Ald and its mutants based on the structure of Mycobacterium tuberculosis MtAld (PDB ID 2VHY)., overview. Residue Lys73 is involved in substrate binding
additional information
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alanine is transported from vegetative cells into heterocysts in the diazotrophic Anabaena filament
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additional information
Alkalihalophilus pseudofirmus OF4
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five highly conserved amino acid residues Arg15, Lys73, Lys75, His96, and Asp269 are potential catalytic residues of L-alanine dehydrogenase from Bacillus pseudofirmus strain OF4. Enzyme structure homology modeling and structure-function analysis, comparison of the partial potential active site of OF4Ald and its mutants based on the structure of Mycobacterium tuberculosis MtAld (PDB ID 2VHY)., overview. Residue Lys73 is involved in substrate binding
-
additional information
Alkalihalophilus pseudofirmus ATCC BAA-2126
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five highly conserved amino acid residues Arg15, Lys73, Lys75, His96, and Asp269 are potential catalytic residues of L-alanine dehydrogenase from Bacillus pseudofirmus strain OF4. Enzyme structure homology modeling and structure-function analysis, comparison of the partial potential active site of OF4Ald and its mutants based on the structure of Mycobacterium tuberculosis MtAld (PDB ID 2VHY)., overview. Residue Lys73 is involved in substrate binding
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additional information
Alkalihalophilus pseudofirmus JCM 17055
-
five highly conserved amino acid residues Arg15, Lys73, Lys75, His96, and Asp269 are potential catalytic residues of L-alanine dehydrogenase from Bacillus pseudofirmus strain OF4. Enzyme structure homology modeling and structure-function analysis, comparison of the partial potential active site of OF4Ald and its mutants based on the structure of Mycobacterium tuberculosis MtAld (PDB ID 2VHY)., overview. Residue Lys73 is involved in substrate binding
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