1887

Abstract

SUMMARY: The malate synthase activity detectable in crude extracts of AM1 has been shown to be due to a coupling of a malyl-CoA hydrolase with malyl-CoA lyase and not due to a discrete malate synthase enzyme. The partial purification of this malyl-CoA hydrolase from AM1 has shown that it is distinct from citrate synthase which also hydrolyses malyl-CoA. The malyl-CoA hydrolase has a low for malyl-GoA (7.0 μM). A mutant of AM1, ICT51 (Taylor & Anthony, 1975), which is unable to grow on ethanol, malonate or 3-hydroxybutyrate, has been shown to have an altered malyl-CoA hydrolase with a for malyl-CoA 30 times higher than that of the enzyme present in the wildtype organism. Two classes of revertants to growth on these substrates have been isolated: (i) those with a malyl-CoA hydrolase of similar to the wild-type and (ii) those in which the malyl-CoA hydrolase activity remains the same as in the mutant ICT51. The nature of the mutation leading to the latter class of revertants is unknown.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-95-1-121
1976-07-01
2020-11-24
Loading full text...

Full text loading...

http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-95-1-121
Loading

Most cited this month Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error