scholarly journals Isolated 2-Methylbutyrylglycinuria Caused by Short/Branched-Chain Acyl-CoA Dehydrogenase Deficiency: Identification of a New Enzyme Defect, Resolution of Its Molecular Basis, and Evidence for Distinct Acyl-CoA Dehydrogenases in Isoleucine And Valine Metabolism

2000 ◽  
Vol 67 (5) ◽  
pp. 1095-1103 ◽  
Author(s):  
Brage Storstein Andresen ◽  
Ernst Christensen ◽  
Thomas J. Corydon ◽  
Peter Bross ◽  
Bente Pilgaard ◽  
...  
Keyword(s):  
Molecular Basis ◽  
Dehydrogenase Deficiency ◽  
Enzyme Defect ◽  
Chain Acyl ◽  
Branched Chain ◽  
Acyl Coa Dehydrogenases

scholarly journals AMP-forming acetyl-CoA synthetases in Archaea show unexpected diversity in substrate utilization

Archaea ◽  
2006 ◽  
Vol 2 (2) ◽  
pp. 95-107 ◽  
Author(s):  
Cheryl Ingram-Smith ◽  
Kerry S. Smith
Keyword(s):  
Phylogenetic Analysis ◽  
Molecular Basis ◽  
Catalytic Efficiency ◽  
Adenosine Monophosphate ◽  
Archaeoglobus Fulgidus ◽  
Acetyl Coa ◽  
Chain Acyl ◽  
Key Enzyme ◽  
Methanothermobacter Thermautotrophicus ◽  
Branched Chain

Adenosine monophosphate (AMP)-forming acetyl-CoA synthetase (ACS; acetate:CoA ligase (AMP-forming), EC 6.2.1.1) is a key enzyme for conversion of acetate to acetyl-CoA, an essential intermediate at the junction of anabolic and catabolic pathways. Phylogenetic analysis of putative short and medium chain acyl-CoA synthetase sequences indicates that the ACSs form a distinct clade from other acyl-CoA synthetases. Within this clade, the archaeal ACSs are not monophyletic and fall into three groups composed of both bacterial and archaeal sequences. Kinetic analysis of two archaeal enzymes, an ACS fromMethanothermobacter thermautotrophicus(designated as MT-ACS1) and an ACS fromArchaeoglobus fulgidus(designated as AF-ACS2), revealed that these enzymes have very different properties. MT-ACS1 has nearly 11-fold higher affinity and 14-fold higher catalytic efficiency with acetate than with propionate, a property shared by most ACSs. However, AF-ACS2 has only 2.3-fold higher affinity and catalytic efficiency with acetate than with propionate. This enzyme has an affinity for propionate that is almost identical to that of MT-ACS1 for acetate and nearly tenfold higher than the affinity of MT-ACS1 for propionate. Furthermore, MT-ACS1 is limited to acetate and propionate as acyl substrates, whereas AF-ACS2 can also utilize longer straight and branched chain acyl substrates. Phylogenetic analysis, sequence alignment and structural modeling suggest a molecular basis for the altered substrate preference and expanded substrate range of AF-ACS2 versus MT-ACS1.

scholarly journals Molecular basis of human mitochondrial very-long-chain acyl-CoA dehydrogenase deficiency causing cardiomyopathy and sudden death in childhood.

1995 ◽  
Vol 92 (23) ◽  
pp. 10496-10500 ◽  
Author(s):  
A. W. Strauss ◽  
C. K. Powell ◽  
D. E. Hale ◽  
M. M. Anderson ◽  
A. Ahuja ◽  
...  
Keyword(s):  
Sudden Death ◽  
Molecular Basis ◽  
Dehydrogenase Deficiency ◽  
Chain Acyl ◽  
Long Chain

Molecular Basis of Isovaleric Acidemia and Medium-Chain Acyl-CoA Dehydrogenase Deficiency

Enzyme ◽  
1987 ◽  
Vol 38 (1-4) ◽  
pp. 91-107 ◽  
Author(s):  
Kay Tanaka ◽  
Yasuyuki Ikeda ◽  
Yoichi Matsubara ◽  
David B. Hamyna
Keyword(s):  
Molecular Basis ◽  
Dehydrogenase Deficiency ◽  
Medium Chain ◽  
Isovaleric Acidemia ◽  
Chain Acyl

Short/branched-chain acyl-CoA dehydrogenase deficiency due to an IVS3+3A>G mutation that causes exon skipping

2005 ◽  
Vol 118 (6) ◽  
pp. 680-690 ◽  
Author(s):  
Pia Pinholt Madsen ◽  
Maria Kibæk ◽  
Xavier Roca ◽  
Ravi Sachidanandam ◽  
Adrian R. Krainer ◽  
...  
Keyword(s):  
Dehydrogenase Deficiency ◽  
Exon Skipping ◽  
Chain Acyl ◽  
Branched Chain

Molecular basis of inherited medium-chain acyl-CoA dehydrogenase deficiency causing sudden child death

1992 ◽  
Vol 15 (2) ◽  
pp. 171-180 ◽  
Author(s):  
D. P. Kelly ◽  
D. E. Hale ◽  
S. L. Rutledge ◽  
M. L. Ogden ◽  
A. J. Whelan ◽  
...  
Keyword(s):  
Molecular Basis ◽  
Dehydrogenase Deficiency ◽  
Child Death ◽  
Medium Chain ◽  
Chain Acyl

scholarly journals Effects of riboflavin deficiency and clofibrate treatment on the five acyl-CoA dehydrogenases in rat liver mitochondria

1988 ◽  
Vol 254 (2) ◽  
pp. 477-481 ◽  
Author(s):  
K Veitch ◽  
J P Draye ◽  
F Van Hoof ◽  
H S A Sherratt
Keyword(s):  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Straight Chain ◽  
Riboflavin Deficiency ◽  
Deficient Diet ◽  
Mitochondrial Fractions ◽  
Chain Acyl ◽  
Branched Chain ◽  
Acyl Coa Dehydrogenases ◽  
Riboflavin Deficient

Rats were maintained on a riboflavin-deficient diet or on a diet containing clofibrate (0.5%, w/w). The activities of the mitochondrial FAD-dependent straight-chain acyl-CoA dehydrogenases (butyryl-CoA, octanoyl-CoA and palmitoyl-CoA) and the branched-chain acyl-CoA dehydrogenases (isovaleryl-CoA and isobutyryl-CoA) involved in the degradation of branched-chain acyl-CoA esters derived from branched-chain amino acids were assayed in liver mitochondrial extracts prepared in the absence and presence of exogenous FAD. These activities were low in livers from riboflavin-deficient rats (11, 28, 16, 6 and less than 2% of controls respectively) when prepared in the absence of exogenous FAD, and were not restored to control values when prepared in 25 microM-FAD (29, 47, 28, 7 and 17%). Clofibrate feeding increased the activities of butyryl-CoA, octanoyl-CoA and palmitoyl-CoA dehydrogenases (by 48, 116 and 98% of controls respectively), but not, by contrast, the activities of isovaleryl-CoA and isobutyryl-CoA dehydrogenases (62 and 102% of controls respectively). The mitochondrial fractions from riboflavin-deficient and from clofibrate-fed rats oxidized palmitoylcarnitine in State 3 at rates of 32 and 163% respectively of those from control rats.

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