Kinetic, circular dichroism and fluorescence studies on heterologously expressed carnitine palmitoyltransferase II.
J Enzyme Inhib
; 9(4): 303-8, 1995.
Article
in En
| MEDLINE
| ID: mdl-8598540
ABSTRACT
Km estimates for carnitine and palmitoyl-CoA of heterologously expressed rat liver carnitine palmitoyl-transferase-II (rCPT-II) were 950 +/- 27 microM and 34 +/- 6 microM, respectively. Vmax for the enzyme was 1.8 mumol/min/mg purified protein. Consistent with an ordered reaction mechanism in which palmitoyl-CoA binds first, SDZ CPI 975, a reversible carnitine palmitoyltransferase inhibitor containing both carnitine and alkyl moieties, inhibited rCPT-II competitively with carnitine and uncompetitively with palmitoyl-CoA. Substrate-enzyme interactions were examined by circular dichroism (CD) and fluorescence. Both carnitine and palmitoyl-CoA alone induced conformational changes in the enzyme; dissociation constant estimates by CD for carnitine and palmitoyl-CoA were 41 +/- 5 microM and 7 +/- 2 microM, respectively.
Search on Google
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Mitochondria, Liver
/
Carnitine O-Palmitoyltransferase
Limits:
Animals
Language:
En
Journal:
J Enzyme Inhib
Journal subject:
BIOQUIMICA
Year:
1995
Document type:
Article
Affiliation country:
Estados Unidos