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evolution
several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining. Evolutionary history of CBL
evolution
several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining. Evolutionary history of CBL
evolution
several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining. Evolutionary history of CBL
evolution
several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining. Evolutionary history of CBL
evolution
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several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining. Evolutionary history of CBL
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malfunction
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enzyme inhibition reduces renal injuries due to cisplatin in rats. The cytotoxicity of cisplatin is dependent on the expression level of enzyme mRNA in the respective renal cells
malfunction
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the cytotoxicity of cisplatin is dependent on the expression level of enzyme mRNA in the respective renal cells
malfunction
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the cytotoxicity of cisplatin is dependent on the expression level of enzyme mRNA in the respective renal cells
malfunction
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the cytotoxicity of cisplatin is dependent on the expression level of enzyme mRNA in the respective renal cells
malfunction
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the cytotoxicity of cisplatin is dependent on the expression level of enzyme mRNA in the respective renal cells
malfunction
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the cytotoxicity of cisplatin is dependent on the expression level of enzyme mRNA in the respective renal cells
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malfunction
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the cytotoxicity of cisplatin is dependent on the expression level of enzyme mRNA in the respective renal cells
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malfunction
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enzyme inhibition reduces renal injuries due to cisplatin in rats. The cytotoxicity of cisplatin is dependent on the expression level of enzyme mRNA in the respective renal cells
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malfunction
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the cytotoxicity of cisplatin is dependent on the expression level of enzyme mRNA in the respective renal cells
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metabolism
cystathionine beta-lyase is part of the CYS3-controlled regulatory network
metabolism
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the enzyme may play a crucial role in the metabolism of platinum-cysteine conjugates
metabolism
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the enzyme may play a crucial role in the metabolism of platinum-cysteine conjugates
metabolism
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the enzyme may play a crucial role in the metabolism of platinum-cysteine conjugates
metabolism
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the enzyme may play a crucial role in the metabolism of platinum-cysteine conjugates
metabolism
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the enzyme may play a crucial role in the metabolism of platinum-cysteine conjugates
metabolism
molecular relationship between cystathionine beta-lyase and mimosinase (UniProt ID U6BYK3, EC 3.5.1.61). The recombinant Mp mimosinase degrades both mimosine and cystathionine with a much higher turnover number for mimosine compared with cystathionine, and Mp CBL utilizes only cystathionine as a substrate
metabolism
several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
metabolism
several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
metabolism
several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
metabolism
several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
metabolism
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several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
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metabolism
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several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
-
metabolism
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the enzyme may play a crucial role in the metabolism of platinum-cysteine conjugates
-
metabolism
-
several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
-
metabolism
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the enzyme may play a crucial role in the metabolism of platinum-cysteine conjugates
-
metabolism
-
several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
-
metabolism
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the enzyme may play a crucial role in the metabolism of platinum-cysteine conjugates
-
metabolism
-
several bacteria with reduced genomes lack alr, encoding alanine racemase (EC 5.1.1.1), but contain metC encoding cystathionine beta-lyase (CBL), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
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metabolism
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the enzyme may play a crucial role in the metabolism of platinum-cysteine conjugates
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physiological function
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expression in cells colonized in mice. CBL appears to be over-expressed in vivo after 2 and 6 h of infection
physiological function
cystathionine beta-lyase performs an essential role in the transsulfuration pathway by its primary reaction of forming homocysteine from cystathionine. It allows for the utilization of the intracellular pool of cystathionine for the synthesis of homocysteine which serves as the immediate precursor to methionine
physiological function
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RNAi knockdown of the enzyme has no effect on phenotype
physiological function
enzyme catalyzes the transamination of kynurenine to kynurenic acid, and is identical to cysteine conjugate beta-lyase 2 and glutamine transaminase L. It is more efficient in transamination of glutamine with indo-3-pyruvate or oxaloacetate as aminogroup acceptor than the mouse KAT1
additional information
conserved residues W188 and W340 are situated at the core of the domain interface that forms the active-site cleft, W188 is a useful probe of subtle conformational changes at the domain interface and active site. The active site, containing the pyridoxal 5'-phosphate cofactor is situated at the interface between the catalytic (residues 61-256) and C-terminal (residues 257-395) domains. The N-terminal domain (residues 1-60) contributes to the active site of the neighboring subunit
additional information
cystathionine gamma-synthase, EC 2.5.1.48, and cystathionine beta-lyase sequence and structure comparison, both belonging to the gamma-subfamily of fold-type I, overview
additional information
structural modeling of Ls-MalY, structure comparisons, overview
additional information
homology modeling and molecular dynamics simulations of Mp CBL. Active site structure
additional information
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homology modeling and molecular dynamics simulations of Mp CBL. Active site structure
additional information
comparisons of structure and function of CBL and ALR, overview
additional information
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structural modeling of Ls-MalY, structure comparisons, overview
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