The enzyme, characterized from the bacteria Pseudomonas aeruginosa and Chromohalobacter salexigens, is involved in a degradation pathway of glycine betaine. It is composed of two subunits - a ferredoxin reductase component that contains FAD, and a terminal oxygenase component that contains a [2Fe-2S] Rieske-type iron-sulfur cluster and a nonheme iron centre.
The enzyme appears in viruses and cellular organisms
The enzyme, characterized from the bacteria Pseudomonas aeruginosa and Chromohalobacter salexigens, is involved in a degradation pathway of glycine betaine. It is composed of two subunits - a ferredoxin reductase component that contains FAD, and a terminal oxygenase component that contains a [2Fe-2S] Rieske-type iron-sulfur cluster and a nonheme iron centre.
in the presence of BmoB, NADH, and flavin, BmoA can aerobically degrade glycine betaine to dimethylglycine with the concomitant production of formaldehyde. BmoA exhibits strict substrate specificity for glycine betaine, and its demethylation activity is stimulated by Fe2+
in the presence of BmoB, NADH, and flavin, BmoA can aerobically degrade glycine betaine to dimethylglycine with the concomitant production of formaldehyde. BmoA exhibits strict substrate specificity for glycine betaine, and its demethylation activity is stimulated by Fe2+
PA5410 gene encodes a protein with homology to the large subunit of bacterial hydroxylating dioxygenases. The PA5411 gene encodes a probable flavin adenine dinucleotide-binding ferrodoxin reductase. A strain lacking the genes A5410/PA5411 is defective in growth on choline or glycine betaine but can grow on dimethylglycine. When grown in minimal medium with glucose or pyruvate as the sole carbon source, the growth rate of the mutant strain is indistinguishable from wild-type. The PA5410 and PA5411 genes are also necessary for the utilization of choline and glycine betaine as sole nitrogen sources but are not required for the utilization dimethylglycine, sarcosine, or lysine
deletion of the GbcAB betaine catabolism genes reduces osmotolerance at a high osmolarity. At high osmolarity, the mutant lacking GbcAB accumulates high betaine levels and low endogenous solutes and exhibits reduced expression of the solute synthesis genes. The GbcAB mutant and a mutant deficient in the synthesis of the compatible solutes NAGGN and trehalose exhibit similar reductions in osmotolerance and also in fitness on bean leaves. Activation of betaine catabolism at high osmotic stress results, in part, from induction of transcriptional activator GbdR
enzyme is involved in a degradation pathway of glycine betaine. Escherichia coli expressing Bmoa/BmoB accumulates dimethylglycine. BmoB is an NADH-dependent flavin reductase with one noncovalently bound flavin adenine dinucleotide (FAD) as its prosthetic group
enzyme is involved in a degradation pathway of glycine betaine. Escherichia coli expressing Bmoa/BmoB accumulates dimethylglycine. BmoB is an NADH-dependent flavin reductase with one noncovalently bound flavin adenine dinucleotide (FAD) as its prosthetic group
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
BmoA-His6 solution is very unstable and maintains no more than 10% residual activity when stored for 2 weeks at -40°C in elution buffer with no addition of enzyme stabilizer
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
betaine catabolism is subject to partial repression by succinate under hyperosmotic stress conditions, in contrast to strong repression in the absence of stress
Glycine betaine monooxygenase, an unusual Riesketype oxygenase system, catalyzes the oxidative N-demethylation of glycine betaine in Chromohalobacter salexigens DSM 3043
Appl. Environ. Microbiol.
84
e00377-18
2018
Chromohalobacter israelensis (Q1QYU6 and Q1QYU7), Chromohalobacter israelensis DSM 3043 (Q1QYU6 and Q1QYU7)
Glycine betaine catabolism contributes to Pseudomonas syringae tolerance to hyperosmotic stress by relieving betaine-mediated suppression of compatible solute synthesis