![]() L-ALANINE DEHYDROGENASE structure
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Common Name | L-ALANINE DEHYDROGENASE | ||
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CAS Number | 9029-06-5 | Molecular Weight | N/A | |
Density | N/A | Boiling Point | N/A | |
Molecular Formula | N/A | Melting Point | N/A | |
MSDS | Chinese USA | Flash Point | N/A |
Structural studies of the final enzyme in the alpha-aminoadipate pathway-saccharopine dehydrogenase from Saccharomyces cerevisiae.
J. Mol. Biol. 373(3) , 745-54, (2007) The 1.64 A structure of the apoenzyme form of saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae shows the enzyme to be composed of two domains with similar dinucleotide binding folds with a deep cleft at the interface. The structure reveals homol... |
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Enzymatic synthesis of some (15)N-labelled L-amino acids.
Isotopes Environ. Health Stud. 46(2) , 249-54, (2010) Our group has developed a stereospecific enzymatic method, which is very efficient for the in vitro synthesis of l-[(15)N]serine, l-[(15)N]methionine and l-[(15)N]glutamic acid. These amino acids were prepared from the corresponding alpha -ketoacids in the su... |
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New classes of alanine racemase inhibitors identified by high-throughput screening show antimicrobial activity against Mycobacterium tuberculosis.
PLoS ONE 6(5) , e20374, (2011) In an effort to discover new drugs to treat tuberculosis (TB) we chose alanine racemase as the target of our drug discovery efforts. In Mycobacterium tuberculosis, the causative agent of TB, alanine racemase plays an essential role in cell wall synthesis as i... |
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Global effects of inactivation of the pyruvate kinase gene in the Mycobacterium tuberculosis complex.
J. Bacteriol. 191(24) , 7545-53, (2009) To better understand the global effects of "natural" lesions in genes involved in the pyruvate metabolism in Mycobacterium bovis, null mutations were made in the Mycobacterium tuberculosis H37Rv ald and pykA genes to mimic the M. bovis situation. Like M. bovi... |
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Alanine dehydrogenase activity is required for adequate progression of phycobilisome degradation during nitrogen starvation in Synechococcus elongatus PCC 7942.
J. Bacteriol. 188(14) , 5258-65, (2006) Degradation of the cyanobacterial light-harvesting antenna, the phycobilisome, is a general acclimation response that is observed under various stress conditions. In this study we identified a novel mutant of Synechococcus elongatus PCC 7942 that exhibits imp... |
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AdeR, a PucR-type transcription factor, activates expression of L-alanine dehydrogenase and is required for sporulation of Bacillus subtilis.
J. Bacteriol. 194(18) , 4995-5001, (2012) The Bacillus subtilis ald gene encodes L-alanine dehydrogenase, which catalyzes the NAD(+)-dependent deamination of L-alanine to pyruvate for the generation of energy and is required for normal sporulation. The transcription of ald is induced by alanine, but ... |
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De novo alanine synthesis by bacteroids of Mesorhizobium loti is not required for nitrogen transfer in the determinate nodules of Lotus corniculatus.
J. Bacteriol. 187(15) , 5493-5, (2005) Deletion of both alanine dehydrogenase genes (aldA) in Mesorhizobium loti resulted in the loss of AldA enzyme activity from cultured bacteria and bacteroids but had no effect on the symbiotic performance of Lotus corniculatus plants. Thus, neither indetermina... |
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Computational active site analysis of molecular pathways to improve functional classification of enzymes.
Proteins 72(1) , 184-96, (2008) This study describes a method to computationally assess the function of homologous enzymes through small molecule binding interaction energy. Three experimentally determined X-ray structures and four enzyme models from ornithine cyclo-deaminase, alanine dehyd... |
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Fed-batch two-phase production of alanine by a metabolically engineered Escherichia coli.
Biotechnol. Lett. 28(20) , 1695-700, (2006) DL-Alanine was produced from glucose in an Escherichia coli pfl pps poxB ldhA aceEF pTrc99A-alaD strain which lacked pyruvate-formate lyase, phosphoenolpyruvate (PEP) synthase, pyruvate oxidase, lactate dehydogenase, components of the pyruvate dehydogenase co... |
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Overexpression, purification, crystallization and preliminary X-ray analysis of Rv2780 from Mycobacterium tuberculosis H37Rv.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64(Pt 5) , 367-70, (2008) Rv2780, an alanine dehydrogenase from Mycobacterium tuberculosis (MtAlaDH), catalyzes the NAD-dependent interconversion of alanine and pyruvate. Alanine dehydrogenase is released into the culture medium in substantial amounts by virulent strains of mycobacter... |