Characterization of glycine sarcosine N-methyltransferase and sarcosine dimethylglycine N-methyltransferase

Article Abstract:

Researchers report the first description of two sarcosine methyltransferases from the halophilic anaerobe Ectothiorhodospira halochloris. These enzymes catalyze the formation of glycine betaine, which is produced in response to a saline habitat in order to maintain osmotic balance.

Methyltransferases

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Active site analysis and stabilization of sarcosine oxidase by the substitution of cysteine residues

Article Abstract:

Site-directed mutagenesis helps substitute two cysteine residues in the hydrophobic regions of sarcosine oxidase. Loss of enzyme activity due to C-to-S mutation at position 318, suggests C-318 as a part of the active site of the enzyme. Enzymatic characteristics of C265R c265D, C265A, and C265S, are similar to those of the wild type, but these mutants exhibit higher stability toward inhibitors. Experimental studies reveal the significant stabilities of these mutants throughout the cultivation of the recombinant strains and in cell extracts.

Analysis, Binding sites (Biochemistry), Active sites (Biochemistry), Microbial mutation

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Analysis of interaction between the Arthrobacter sarcosine oxidase and the coenzyme flavin adenine dinucleotide by site-directed mutagenesis

Article Abstract:

The replacement of aspartate amino acid at the 35th position (D-35) and the amino acids in the motif sequence of the Arthrobacter sp. TE1826 sarcosine oxidase (SoxA) affects the interaction of SoxA with the coenzyme flavin adenine dinucleotide (FAD). Substitution of D-35 with alanine, glutamate or asparagine shows that the SoxA carboxyl-terminal participates in the interaction. Mutation in the G-X-G-X-X-G motif sequence decreases or suppresses the SoxA-FAD interaction. Chloride and bromide ions can reverse the decreased activity of some mutants.

Physiological aspects, Oxidases, Mutation (Biology), Mutation, Coenzymes

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