Electronic Rearrangement Induced by Substrate Analog Binding to the Enoyl-CoA Hydratase Active Site: Evidence for Substrate Activation

Biochemistry ◽  
1994 ◽  
Vol 33 (42) ◽  
pp. 12635-12643 ◽  
Author(s):  
Robert L. D'Ordine ◽  
Peter J. Tonge ◽  
Paul R. Carey ◽  
Vernon E. Anderson
Keyword(s):  
Active Site ◽  
Substrate Activation ◽  
Substrate Analog ◽  
Enoyl Coa Hydratase

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.

Substrate analog inhibition and active site titration of purified recombinant HIV-1 protease

Biochemistry ◽  
1990 ◽  
Vol 29 (1) ◽  
pp. 264-269 ◽  
Author(s):  
Alfredo G. Tomasselli ◽  
Mary K. Olsen ◽  
John O. Hui ◽  
Douglas J. Staples ◽  
Tomi K. Sawyer ◽  
...  
Keyword(s):  
Active Site ◽  
Substrate Analog ◽  
Hiv 1

ChemInform Abstract: SUBSTRATE ANALOG BINDING TO THE COUPLED BINUCLEAR COPPER ACTIVE SITE IN TYROSINASE

1985 ◽  
Vol 16 (43) ◽  
Author(s):  
D. E. WILCOX ◽  
A. G. PORRAS ◽  
Y. T. HWANG ◽  
K. LERCH ◽  
M. E. WINKLER ◽  
...  
Keyword(s):  
Active Site ◽  
Binuclear Copper ◽  
Substrate Analog

Substrate analog binding to the coupled binuclear copper active site in tyrosinase

1985 ◽  
Vol 107 (13) ◽  
pp. 4015-4027 ◽  
Author(s):  
Dean E. Wilcox ◽  
Arturo G. Porras ◽  
Yeong T. Hwang ◽  
Konrad Lerch ◽  
Marjorie E. Winkler ◽  
...  
Keyword(s):  
Active Site ◽  
Binuclear Copper ◽  
Substrate Analog

Involvement of Glycine 141 in Substrate Activation by Enoyl-CoA Hydratase†

Biochemistry ◽  
2001 ◽  
Vol 40 (6) ◽  
pp. 1725-1733 ◽  
Author(s):  
Alasdair F. Bell ◽  
Jiaquan Wu ◽  
Yuguo Feng ◽  
Peter J. Tonge
Keyword(s):  
Substrate Activation ◽  
Enoyl Coa Hydratase

scholarly journals Binding of Alkylurea Inhibitors to Epoxide Hydrolase Implicates Active Site Tyrosines in Substrate Activation

2000 ◽  
Vol 275 (20) ◽  
pp. 15265-15270 ◽  
Author(s):  
Maria A. Argiriadi ◽  
Christophe Morisseau ◽  
Marvin H. Goodrow ◽  
Deanna L. Dowdy ◽  
Bruce D. Hammock ◽  
...  
Keyword(s):  
Active Site ◽  
Epoxide Hydrolase ◽  
Substrate Activation

Synthesis of a new substrate analog of firefly luciferin. Active-site probe

Biochemistry ◽  
1973 ◽  
Vol 12 (10) ◽  
pp. 1845-1852 ◽  
Author(s):  
Lemuel J. Bowie ◽  
Vaclav Horak ◽  
Marlene DeLuca
Keyword(s):  
Active Site ◽  
Substrate Analog ◽  
Firefly Luciferin ◽  
Active Site Probe
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