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Determination of the sequence of the aralkyl acyl-CoA:amino acid N-acyltransferase from bovine liver mitochondria

✍ Scribed by Vessey, Donald A. ;Lau, Eva

Publisher
John Wiley and Sons
Year
1996
Tongue
English
Weight
90 KB
Volume
11
Category
Article
ISSN
0887-2082

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The arylacetyl acyl-CoA:amino acid N-acyltransferase was previously purified to homogeneity from bovine liver mitochondria, and partial sequences were obtained for peptides generated by cyanogen bromide cleavage of the enzyme. One of these sequences was used to design an oligonucleotide probe that w

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The acyl-CoAamino acid N-acyltransferases were partially purified from human liver mitochondria. The aralkyl transferase (ArAlk) had glycine conjugating activity toward the fol- Its kinetic properties and responses to salt were very similar to those of bovine ArAlk. Further, its molecular weight wa

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Neither salicylate nor ibuprofen was a substrate or inhibitor of the long-chain fatty acid:CoA ligase. In contrast, all three xenobiotic-metabolizing medium-chain fatty acid:CoA ligases (XL-I, had activity toward salicylate. The K , value for salicylate was similar for all three forms (2 to 3 pM), b

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## Abstract The purification of xenobiotic/medium‐chain fatty acid:CoA ligases (XM‐ligases) from human liver mitochondria resulted in the isolation of two chromatographically separable forms (HXM‐A and HXM‐B). These two forms were purified to near homogeneity, cleaved with cyanogen bromide, the res