Product Binding Modulates the Thermodynamic Properties of a Megasphaera elsdenii Short-Chain Acyl-CoA Dehydrogenase Active-Site Mutant

Biochemistry ◽  
1994 ◽  
Vol 33 (23) ◽  
pp. 7082-7087 ◽  
Author(s):  
Donald F. Becker ◽  
James A. Fuchs ◽  
Marian T. Stankovich
Keyword(s):  
Thermodynamic Properties ◽  
Active Site ◽  
Short Chain ◽  
Megasphaera Elsdenii ◽  
Chain Acyl

Characterization of wild-type and an active-site mutant in Escherichia coli of short-chain acyl-CoA dehydrogenase from Megasphaera elsdenii

Biochemistry ◽  
1993 ◽  
Vol 32 (40) ◽  
pp. 10736-10742 ◽  
Author(s):  
Donald F. Becker ◽  
James A. Fuchs ◽  
David K. Banfield ◽  
Walter D. Funk ◽  
Ross T. A. MacGillivray ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Active Site ◽  
Short Chain ◽  
Wild Type ◽  
Megasphaera Elsdenii ◽  
Chain Acyl

Functional Role of the Active Site Glutamate-368 in Rat Short Chain Acyl-CoA Dehydrogenase†

Biochemistry ◽  
1996 ◽  
Vol 35 (48) ◽  
pp. 15356-15363 ◽  
Author(s):  
Kevin P. Battaile ◽  
Al-Walid A. Mohsen ◽  
Jerry Vockley
Keyword(s):  
Active Site ◽  
Functional Role ◽  
Short Chain ◽  
Chain Acyl

scholarly journals A Single LC-MS/MS Analysis to Quantify CoA Biosynthetic Intermediates and Short-Chain Acyl CoAs

Metabolites ◽  
2021 ◽  
Vol 11 (8) ◽  
pp. 468
Author(s):  
Anthony E. Jones ◽  
Nataly J. Arias ◽  
Aracely Acevedo ◽  
Srinivasa T. Reddy ◽  
Ajit S. Divakaruni ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Sample Preparation ◽  
Biosynthetic Pathway ◽  
Solid Phase ◽  
High Sensitivity ◽  
Short Chain ◽  
Extraction Column ◽  
Chain Acyl ◽  
Precision And Accuracy ◽  
Mass Spectrometry Mass Spectrometry

Coenzyme A (CoA) is an essential cofactor for dozens of reactions in intermediary metabolism. Dysregulation of CoA synthesis or acyl CoA metabolism can result in metabolic or neurodegenerative disease. Although several methods use liquid chromatography coupled with mass spectrometry/mass spectrometry (LC-MS/MS) to quantify acyl CoA levels in biological samples, few allow for simultaneous measurement of intermediates in the CoA biosynthetic pathway. Here we describe a simple sample preparation and LC-MS/MS method that can measure both short-chain acyl CoAs and biosynthetic precursors of CoA. The method does not require use of a solid phase extraction column during sample preparation and exhibits high sensitivity, precision, and accuracy. It reproduces expected changes from known effectors of cellular CoA homeostasis and helps clarify the mechanism by which excess concentrations of etomoxir reduce intracellular CoA levels.

scholarly journals Redox Properties of Human Medium-Chain Acyl-CoA Dehydrogenase, Modulation by Charged Active-Site Amino Acid Residues†

Biochemistry ◽  
1998 ◽  
Vol 37 (41) ◽  
pp. 14605-14612 ◽  
Author(s):  
Gina J. Mancini-Samuelson ◽  
Volker Kieweg ◽  
Kim Marie Sabaj ◽  
Sandro Ghisla ◽  
Marian T. Stankovich
Keyword(s):  
Amino Acid ◽  
Active Site ◽  
Redox Properties ◽  
Amino Acid Residues ◽  
Medium Chain ◽  
Chain Acyl

Crystal structure of enoyl-CoA hydratase from Thermus thermophilus HB8

2021 ◽  
Vol 77 (5) ◽  
pp. 148-155
Author(s):  
Sivaraman Padavattan ◽  
Sneha Jos ◽  
Hemanga Gogoi ◽  
Bagautdin Bagautdinov
Keyword(s):  
Crystal Structure ◽  
Active Site ◽  
Thermus Thermophilus ◽  
Tca Cycle ◽  
Significant Shift ◽  
Oxidation Pathway ◽  
Ligand Binding Sites ◽  
Chain Acyl ◽  
Α Helix ◽  
Enoyl Coa Hydratase

Fatty-acid degradation is an oxidative process that involves four enzymatic steps and is referred to as the β-oxidation pathway. During this process, long-chain acyl-CoAs are broken down into acetyl-CoA, which enters the mitochondrial tricarboxylic acid (TCA) cycle, resulting in the production of energy in the form of ATP. Enoyl-CoA hydratase (ECH) catalyzes the second step of the β-oxidation pathway by the syn addition of water to the double bond between C2 and C3 of a 2-trans-enoyl-CoA, resulting in the formation of a 3-hydroxyacyl CoA. Here, the crystal structure of ECH from Thermus thermophilus HB8 (TtECH) is reported at 2.85 Å resolution. TtECH forms a hexamer as a dimer of trimers, and wide clefts are uniquely formed between the two trimers. Although the overall structure of TtECH is similar to that of a hexameric ECH from Rattus norvegicus (RnECH), there is a significant shift in the positions of the helices and loops around the active-site region, which includes the replacement of a longer α3 helix with a shorter α-helix and 310-helix in RnECH. Additionally, one of the catalytic residues of RnECH, Glu144 (numbering based on the RnECH enzyme), is replaced by a glycine in TtECH, while the other catalytic residue Glu164, as well as Ala98 and Gly141 that stabilize the enolate intermediate, is conserved. Their putative ligand-binding sites and active-site residue compositions are dissimilar.

scholarly journals First case report of short-chain acyl-CoA dehydrogenase deficiency in China

2013 ◽  
Vol 2013 (Suppl 1) ◽  
pp. P181
Author(s):  
MinYan Jiang ◽  
Li Liu ◽  
MinZhi Peng ◽  
CuiLi Liang ◽  
HuiYing Sheng ◽  
...  
Keyword(s):  
Case Report ◽  
Dehydrogenase Deficiency ◽  
Short Chain ◽  
First Case ◽  
Chain Acyl
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