Maleylacetate reductases in chloroaromatic-degrading bacteria using the modified ortho pathway: comparison of catalytic properties.
The maleylacetate reductases from Pseudomonas aeruginosa RHO1 and Alcaligenes eutrophus JMP134 were tested for activity and affinity to various maleylacetates as well as dechlorinating properties. The dechlorinating activity and the kcat/Km values revealed high-level similarity of these reductases to that of Pseudomonas sp. strain B13.
Bergische Universität-Gesamthochschule Wuppertal, Germany.
D
D
Müller
M
M
Schlömann
W
W
Reineke
D000421:Alcaligenes / Q000201:enzymology*; D001673:Biodegradation, Environmental; D007700:Kinetics; D008298:Maleates / Q000378:metabolism; D008956:Models, Chemical; D009243:NAD / Q000378:metabolism; D010088:Oxidoreductases / Q000378:metabolism*; D044925:Oxidoreductases Acting on CH-CH Group Donors; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D013379:Substrate Specificity
D008298:Maleates; D009243:NAD; C011905:maleoylacetic acid; D010088:Oxidoreductases; D044925:Oxidoreductases Acting on CH-CH Group Donors; C021530:maleylacetate reductase