scholarly journals Potential steps in the evolution of a fused trimeric all-β dUTPase involve a catalytically competent fused dimeric intermediate

FEBS Journal ◽  
2016 ◽  
Vol 283 (18) ◽  
pp. 3268-3286 ◽  
Author(s):  
András Benedek ◽  
András Horváth ◽  
Rita Hirmondó ◽  
Olivér Ozohanics ◽  
Angéla Békési ◽  
...  
Keyword(s):  
Dimeric Intermediate

Identification of a Dimeric Intermediate in the Unfolding Pathway for the Calcium-Binding Protein S100B

2008 ◽  
Vol 382 (4) ◽  
pp. 1075-1088 ◽  
Author(s):  
Gary S. Shaw ◽  
Nicole M. Marlatt ◽  
Peter L. Ferguson ◽  
Kathryn R. Barber ◽  
Stephen P. Bottomley
Keyword(s):  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Dimeric Intermediate ◽  
Protein S100b

scholarly journals Comparing the folding landscapes of evolutionarily divergent procaspase-3

2022 ◽  
Author(s):  
Liqi Yao ◽  
Clay Clark
Keyword(s):  
Conformational Change ◽  
Common Ancestor ◽  
Folding Pathway ◽  
Free Energies ◽  
Folding Intermediates ◽  
Effector Caspases ◽  
The Common ◽  
Ph Dependent ◽  
Species Specific ◽  
Dimeric Intermediate

All caspases evolved from a common ancestor and subsequently developed into two general classes, inflammatory or apoptotic caspases. The caspase-hemoglobinase fold has been conserved throughout nearly one billion years of evolution and is utilized for both the monomeric and dimeric subfamilies of apoptotic caspases, called initiator and effector caspases, respectively. We compared the folding and assembly of procaspase-3b from zebrafish to that of human effector procaspases in order to examine the conservation of the folding landscape. Urea-induced equilibrium folding/unfolding of procaspase-3b showed a minimum three-state folding pathway, where the native dimer isomerizes to a partially folded dimeric intermediate, which then unfolds. A partially folded monomeric intermediate observed in the folding landscape of human procaspase-3 is not well-populated in zebrafish procaspase-3b. By comparing effector caspases from different species, we show that the effector procaspase dimer undergoes a pH-dependent conformational change, and that the conformational species in the folding landscape exhibit similar free energies. Together, the data show that the landscape for the caspase-hemoglobinase fold is conserved, yet it provides flexibility for species-specific stabilization or destabilization of folding intermediates resulting in changes in stability. The common pH-dependent conformational change in the native dimer, which yields an enzymatically inactive species, may provide an additional, albeit reversible, mechanism for controlling caspase activity in the cell.

Evidence of a Thermal Unfolding Dimeric Intermediate for the Escherichia coli Histone-like HU Proteins: Thermodynamics and Structure

2003 ◽  
Vol 331 (1) ◽  
pp. 101-121 ◽  
Author(s):  
Jean Ramstein ◽  
Nadège Hervouet ◽  
Franck Coste ◽  
Charles Zelwer ◽  
Jacques Oberto ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Thermal Unfolding ◽  
Hu Proteins ◽  
Dimeric Intermediate

Biosynthesis of the lupine alkaloids. I. Lupinine

1985 ◽  
Vol 63 (10) ◽  
pp. 2707-2718 ◽  
Author(s):  
W. Marek Golebiewski ◽  
Ian D. Spenser
Keyword(s):  
Nmr Spectroscopy ◽  
H Nmr ◽  
Dimeric Intermediate ◽  
C Nmr

The mode of incorporation into lupinine of cadaverine, intramolecularly doubly labelled with,15N and with,13C at the C-atom adjacent to 15N, i.e., 13C, 15N-"bond-labelled", was determined by,13C nmr spectroscopy; lupinine is generated from two cadaverine-derived C5-units by a route which excludes a "dimeric" intermediate with C2v symmetry. The mode of incorporation of 2H from L-(2-2H)lysine, from (R)- and (S)-(1-2H)cadaverine, and from (2-2H)-Δ1-piperideine into lupinine was determined by 2H nmr spectroscopy. The results corroborate the conclusions from the 13C,15N experiment and they establish the stereochemistry of six of the steps in the biosynthetic conversion of L-lysine into lupinine.

The dimeric intermediate on the pathway of reconstitution of lactate dehydrogenase is enzymatically active

FEBS Letters ◽  
1983 ◽  
Vol 163 (1) ◽  
pp. 132-135 ◽  
Author(s):  
Rainer Girg ◽  
Rainer Rudolph ◽  
Rainer Jaenicke
Keyword(s):  
Lactate Dehydrogenase ◽  
Dimeric Intermediate

scholarly journals Activation of Initiator Caspases through a Stable Dimeric Intermediate

2002 ◽  
Vol 277 (52) ◽  
pp. 50761-50767 ◽  
Author(s):  
Min Chen ◽  
Aaron Orozco ◽  
David M. Spencer ◽  
Jin Wang
Keyword(s):  
Initiator Caspases ◽  
Dimeric Intermediate

Use of a Diimidoester Cross-Linking Reagent to Examine the Submit Structure of Rabbit Muscle Pyruvate Kinase

1972 ◽  
Vol 50 (4) ◽  
pp. 416-422 ◽  
Author(s):  
Gregg E. DaVies ◽  
J. Gordin Kaplan
Keyword(s):  
Pyruvate Kinase ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Cross Linking ◽  
Rabbit Muscle ◽  
Cross Links ◽  
Primary Amino ◽  
Muscle Pyruvate Kinase ◽  
Dimeric Intermediate ◽  
Hydrolysis Of

Rabbit muscle pyruvate kinase, a tetramer of highly similar or identical subunits, is known to dissociate in urea via a dimeric intermediate. To provide additional evidence regarding the structure of the native oligomer, we have treated pyruvate kinase with dimethyl pimelimidate and examined the yields of cross-linked species resolved by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. Of four products resolved, predominating species are dimers and tetramers of the pyruvate kinase subunit, while monomers and trimers are present in lesser amounts. These relative yields are consistent with a dimeric structure of the tetramer.In a typical cross-linking reaction, about 86 of the 148 primary amino groups in the pyruvate kinase tetramer are amidinated. Of 53 moles of cross-linking reagent incorporated per mole of tetramer, 38% have reacted monofunctionally, with hydrolysis of the second imidoester group, and 62% have reacted bifunctionally to form intra- and intersubunit cross-links.

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