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Amino Acid Bio Synthesis | Biosynthesis | Alanine

N2 - D-Alanine is a structural component of mycobacterial peptidoglycan. The primary route of D-alanine biosynthesis in eubacteria is the enantiomeric conversion from L-alanine, a reaction catalysed by D-alanine racemase (Alr). Mycobacterium smegmatis alr insertion mutants are not dependent on D-alanine for growth and display a metabolic pattern consistent with an alternative pathway for D-alanine biosynthesis. In this study, we demonstrate that the M. smegmatis alr insertion mutant TAM23 can synthesize D-alanine at lower levels than the parental strain. The insertional inactivation of the alr gene also decreases the intracellular survival of mutant strains within primary human monocyte-derived macrophages. By complementation studies, we confirmed that the impairment of alr gene function is responsible for this reduced survival. Inhibition of superoxide anion and nitric oxide formation in macrophages suppresses the differential survival. In contrast, for bacteria grown in broth, both strains had approximately the same susceptibility to hydrogen peroxide, acidified sodium nitrite, low pH and polymyxin B. In contrast, TAM23 exhibited increased resistance to lysozyme. D-Alanine supplementation considerably increased TAM23 viability in nutritionally deficient media and within macrophages. These results suggest that nutrient deprivation in phagocytic cells combined with killing mediated by reactive intermediates underlies the decreased survival of alr mutants. This knowledge may be valuable in the construction of mycobacterial auxotrophic vaccine candidates.

Purification and properties of L-alanine aminotransferase from Chlamydomonas reinhardtii.

The biosynthesis of fumonisin B1 by Fusarium moniliforme was studied in liquid culture. Stable isotope labeled alanine was added as a precursor to static and shaken cultures of F. moniliforme. Incorporation of13C and2H labeled L-alanine into fumonisin B1 was measured by GC-MS. Under static culture conditions, 20.8 μg ml-1 of FB1 were produced with a 5.5% level of incorporation of intact, labeled alanine into fumonisin B1. Under shake culture conditions, much higher levels of fumonisin B1 were produced with levels reaching 159-240 μg ml-1 by 21 days after culture initiation. A lower level of alanine incorporation, from 1.1-1.4%, was observed under these conditions. Under shake conditions, incorporation of labeled alanine was reduced because of the rapid metabolism of these cultures combined with the high level of fumonisin B1 production resulted in rapid turnover of the added, labeled alanine and reduced percentage of incorporation. The evidence presented indicates that alanine is incorporated intact into fumonisin B1.

β-Alanine Biosynthesis in Methanocaldococcus jannaschii

Alanine aminotransferase catalyses the breakdown of alanine after hypoxia in Arabidopsis thaliana.

Differences in properties between aromatic amino acid: aromatic keto acid aminotransferases and aromatic amino acid: alpha-ketoglutarate aminotransferases.

Alanine:glyoxylate aminotransferase (EC 2.6.1.44), which is involved in the glyoxylate pathway of glycine and serine biosynthesis from tricarboxylic acid-cycle intermediates in Saccharomyces cerevisiae, was highly purified and characterized. The enzyme had M(r) about 80,000, with two identical subunits. It was highly specific for L-alanine and glyoxylate and contained pyridoxal 5'-phosphate as cofactor. The apparent K(m) values were 2.1mM and 0.7 mM for L-alanine and glyoxylate respectively. The activity was low (10 nmol/min per mg of protein) with glucose as sole carbon source, but was remarkably high with ethanol or acetate as carbon source (930 and 430 nmol/min per mg respectively). The transamination of glyoxylate is mainly catalysed by this enzyme in ethanol-grown cells. When glucose-grown cells were incubated in medium containing ethanol as sole carbon source, the activity markedly increased, and the increase was completely blocked by cycloheximide, suggesting that the enzyme is synthesized de novo during the incubation period. Similarity in the amino acid composition was observed, but immunological cross-reactivity was not observed among alanine:glyoxylate aminotransferases from yeast and vertebrate liver.

22/04/2017 · Alanine Biosynthesis Catalyst University

coli L-phenylalanine pathway for the production of D-phenylglycine (D-Phg).

Purification and characterization of the alanine aminotransferase from the hyperthermophilic Archaeon pyrococcus furiosus and its role in alanine production.

Stimulation of alanine amino transferase (AlaAT) gene expression and alanine accumulation in embryo axis of the model legume Medicago truncatula contribute to anoxia stress tolerance.

Identity with alanine:glyoxylate aminotransferase and serine:pyruvate aminotransferase.
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(Pyruvate Conversion to L-Alanine) - Duration: 16:16

AB - Alanine:glyoxylate aminotransferase (EC 2.6.1.44), which is involved in the glyoxylate pathway of glycine and serine biosynthesis from tricarboxylic acid-cycle intermediates in Saccharomyces cerevisiae, was highly purified and characterized. The enzyme had M(r) about 80,000, with two identical subunits. It was highly specific for L-alanine and glyoxylate and contained pyridoxal 5'-phosphate as cofactor. The apparent K(m) values were 2.1mM and 0.7 mM for L-alanine and glyoxylate respectively. The activity was low (10 nmol/min per mg of protein) with glucose as sole carbon source, but was remarkably high with ethanol or acetate as carbon source (930 and 430 nmol/min per mg respectively). The transamination of glyoxylate is mainly catalysed by this enzyme in ethanol-grown cells. When glucose-grown cells were incubated in medium containing ethanol as sole carbon source, the activity markedly increased, and the increase was completely blocked by cycloheximide, suggesting that the enzyme is synthesized de novo during the incubation period. Similarity in the amino acid composition was observed, but immunological cross-reactivity was not observed among alanine:glyoxylate aminotransferases from yeast and vertebrate liver.

AMINO ACID BIOSYNTHESIS (AA-1).pdf | Biosynthesis | Alanine

N2 - Alanine:glyoxylate aminotransferase (EC 2.6.1.44), which is involved in the glyoxylate pathway of glycine and serine biosynthesis from tricarboxylic acid-cycle intermediates in Saccharomyces cerevisiae, was highly purified and characterized. The enzyme had M(r) about 80,000, with two identical subunits. It was highly specific for L-alanine and glyoxylate and contained pyridoxal 5'-phosphate as cofactor. The apparent K(m) values were 2.1mM and 0.7 mM for L-alanine and glyoxylate respectively. The activity was low (10 nmol/min per mg of protein) with glucose as sole carbon source, but was remarkably high with ethanol or acetate as carbon source (930 and 430 nmol/min per mg respectively). The transamination of glyoxylate is mainly catalysed by this enzyme in ethanol-grown cells. When glucose-grown cells were incubated in medium containing ethanol as sole carbon source, the activity markedly increased, and the increase was completely blocked by cycloheximide, suggesting that the enzyme is synthesized de novo during the incubation period. Similarity in the amino acid composition was observed, but immunological cross-reactivity was not observed among alanine:glyoxylate aminotransferases from yeast and vertebrate liver.

Beta-alanine synthesis in Escherichia coli.

Comparative characterization of Aedes 3-hydroxykynurenine transaminase/alanine glyoxylate transaminase and Drosophila serine pyruvate aminotransferase.

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