Evolution of Dichloromethane Utilization

Leisinger, Thomas; Mägli, Andreas; Schimid-Appert, Monika; Zoller, Kurt; Vuilleumier, Stéphane

doi:10.1007/978-94-009-0213-8_35

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Yet More Versatility: Bacterial Gst Enzymes1

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1996

1997

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Cited by 3 publications

(1 citation statement)

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“…DCMD genes from more than a dozen methylotrophic strains originally isolated from sites contaminated with DCM were shown to be located on a 4.2-kb BamHI fragment (50,74), suggesting that propagation of DCM utilization genes may have occurred by horizontal transfer. A recent sequence analysis of a 10-kb gene region including the dcmA gene from strain DM4 revealed the presence of three different insertion elements upstream and downstream of the gene for DCMD/ GST (50,74).…”

Section: Yet More Versatility: Bacterial Gst Enzymesmentioning

confidence: 99%

Bacterial glutathione S-transferases: what are they good for?

1997

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Section: Yet More Versatility: Bacterial Gst Enzymesmentioning

confidence: 99%

Bacterial glutathione S-transferases: what are they good for?

1997

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Biodegradation of chlorinated aliphatic compounds

Leisinger

1996

Current Opinion in Biotechnology

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Protein Engineering Studies of Dichloromethane Dehalogenase/Glutathione S‐Transferase from Methylophilus Sp. Strain DM11

Vuilleumier

Leistnger

1996

European Journal of Biochemistry

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The structural gene for dichloromethane dehalogenase/glutathione S-transferase (GST, EC 2.5.1.18) from Methylophilus sp. strain DM1 1 was subcloned into a multicopy plasmid under the control of the T7 polymerase promoter, allowing expression in Escherichia coli and easy purification of the enzyme in good yield. Several point mutations leading to amino acid changes at residues Tyr6, His8 and Serl2 of the protein were introduced in this gene. Mutations at Tyr6, the N-terminal tyrosine known to be essential for enzymatic activity in glutathione S-transferases of the a, and n classes, had little effect on the activity of dichloromethane dehalogenase. The same applied for mutations at residue H i d , which from multiple alignments of GST sequences may also correspond to the conserved N-terminal tyrosine residue of GST enzymes. The higher turnover rate of the wild-type enzyme with dibromomethane compared with dichloromethane was lost in mutants with amino acid replacements at residue Hiss, but retained in mutant proteins at Tyr6. Mutations at Serl2 led to mutants with drastically reduced enzymatic activity, pinpointing this residue as an essential determinant of catalytic efficiency.

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Evolution of Dichloromethane Utilization

Cited by 3 publications

References 17 publications

Bacterial glutathione S-transferases: what are they good for?

Bacterial glutathione S-transferases: what are they good for?

Biodegradation of chlorinated aliphatic compounds

Protein Engineering Studies of Dichloromethane Dehalogenase/Glutathione S‐Transferase from Methylophilus Sp. Strain DM11

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