Selective inhibition of lignoceroyl-CoA synthetase by adenosine 5′-alkylphosphates
نویسندگان
چکیده
منابع مشابه
Inhibition by Adenosine 5'-Triphosphate
Two major species of glucose-6-phosphate dehydrogenase (EC 1.1.1.49) differing in size, pyridine nucleotide specificity, and susceptibility to inhibition by adenosine 5'-triphosphate (ATP) were detected in extracts of Pseudomonas multivorans (which has recently been shown to be synonymous with the species Pseudomonas cepacia) ATCC 17616. The large species (molecular weight ca. 230,000) was acti...
متن کاملAdenosine 5'-tetraphosphate and adenosine 5'-pentaphosphate are synthesized by yeast acetyl coenzyme A synthetase.
Yeast (Saccharomyces cerevisiae) acetyl coenzyme A (CoA) synthetase (EC 6.2.1.1) catalyzes the synthesis of adenosine 5'-tetraphosphate (P4A) and adenosine 5'-pentaphosphate (p5A) from ATP and tri- or tetrapolyphosphate (P3 or P4), with relative velocities of 7:1, respectively. Of 12 nucleotides tested as potential donors of nucleotidyl moiety, only ATP, adenosine-5'-O-[3-thiotriphosphate], and...
متن کاملPeroxisomal lignoceroyl-CoA ligase deficiency in childhood adrenoleukodystrophy and adrenomyeloneuropathy.
We previously reported that in childhood adrenoleukodystrophy (C-ALD) and adrenomyeloneuropathy (AMN), the peroxisomal beta-oxidation system for very long chain (greater than C22) fatty acids is defective. To further define the defect in these two forms of X chromosome-linked ALD, we examined the oxidation of [1-14C]lignoceric acid (n-tetracosanoic acid, C24:0) and [1-14C]lignoceroyl-CoA (subst...
متن کاملCellular oxidation of lignoceric acid is regulated by the subcellular localization of lignoceroyl-CoA ligases.
The acyl-CoA ligases convert free fatty acids to acyl-CoA derivatives, and these enzymes have been shown to be present in mitochondria, peroxisomes, and endoplasmic reticulum. Because their activity is obligatory for fatty acid metabolism, it is important to identify their substrate specificities and subcellular distributions to further understand the cellular regulation of these pathways. To d...
متن کاملAdenosine 5 ’ - 0 - ( 3 - Thio ) triphosphate , a Substrate and Potent Inhibitor of Escherichia coli Succinyl - CoA Synthetase
Adenosine 5’-0-(3-thio)triphosphate (ATPrS) has been shown to be a potent inhibitor of Escherichia coli succinyl-CoA synthetase. This inhibition was competitive with respect to ATP and GTP (Ki values of 0.8 and 0.7 PM, respectively) and mixed with respect to CoA and succinate. ATP-yS previously had been shown to be a weak substrate of the enzyme, probably because of the relatively sluggish rea...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1994
ISSN: 0014-5793
DOI: 10.1016/0014-5793(94)00992-9