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5.4.99.64
malfunction
mutase from strain DSM 2912 catalyzes isomerization of (R)-3-hydroxybutanoyl-CoA about 7000 times more efficiently than the mutase from Aquincola tertiaricarbonis L108. The most striking structural difference between the two mutases, likely determining stereospecificity, is a replacement of active-site residue Asp found in strain L108 at position 117 with Val in the enzyme from strain DSM 2912, resulting in a reversed polarity at this binding site
737504
5.4.99.64
metabolism
the enzym plays a central role in the degradation of assorted substrates containing a tert-butyl moiety
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736409
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