New insights into the mitochondrial carnitine palmitoyltransferase enzyme system
| Autor: | Keith F. Woeltje, Daniel W. Foster, Victoria Esser, A. Sen, J. D. McGarry, B C Weis |
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| Rok vydání: | 1991 |
| Předmět: |
endocrine system
endocrine system diseases Molecular Sequence Data Mitochondria Liver Mitochondrion Biology Biochemistry Isozyme Models Biological Mitochondria Heart Structure-Activity Relationship Complementary DNA medicine Animals Humans heterocyclic compounds Carnitine O-palmitoyltransferase Carnitine Amino Acid Sequence neoplasms Peptide sequence chemistry.chemical_classification Carnitine O-Palmitoyltransferase Protein primary structure General Medicine digestive system diseases Amino acid Mitochondria Mitochondria Muscle Isoenzymes Malonyl Coenzyme A chemistry medicine.drug |
| Zdroj: | Biochimie. 73(1) |
| ISSN: | 0300-9084 |
| Popis: | Dissection of the mitochondrial carnitine palmitoyltransferase (CPT) enzyme system in terms of its structure/function relationships has proved to be a formidable task. Although no one formulation has gained universal agreement we believe that the weight of evidence supports a model with the following features: a) in any given tissue CPT I and CPT II are distinct proteins; b) CPT I, unlike CPT II, is detergent labile; c) within a species CPT II is expressed body wide, whereas CPT I exists as tissue specific isoforms; d) malonyl-CoA and other CPT I inhibitors probably interact at the catalytic center of the enzyme, not with a regulatory subunit. The amino acid sequences of rat and human CPT II (deduced from cDNA clones) show them to be similar proteins (greater than 80% identity) but encoded by mRNAs of significantly different sizes. Efforts to clone and sequence the cDNA for rat liver CPT I are presently underway. |
| Databáze: | OpenAIRE |
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