Results 21 to 30 of about 21,208,579 (315)

Substitutions at a rheostat position in human aldolase A cause a shift in the conformational population

open access: yesProtein Science, 2021
Some protein positions play special roles in determining the magnitude of protein function: at such “rheostat” positions, varied amino acid substitutions give rise to a continuum of functional outcomes, from wild type (or enhanced), to intermediate, to ...
Kathryn D Fenton   +6 more
semanticscholar   +1 more source

Aldolase A deficiency: Report of new cases and literature review

open access: yesMolecular Genetics and Metabolism Reports, 2021
Aldolase A (ALDOA), is the predominant isoform of aldolase in skeletal muscle and erythrocytes that catalyzes the reversibleconversion of fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate.
C. Papadopoulos   +6 more
doaj   +1 more source

Characterization of fructose-1,6-bisphosphate aldolase during anoxia in the tolerant turtle, Trachemys scripta elegans: an assessment of enzyme activity, expression and structure. [PDF]

open access: yesPLoS ONE, 2013
One of the most adaptive facultative anaerobes among vertebrates is the freshwater turtle, Trachemys scripta elegans. Upon a decrease in oxygen supply and oxidative phosphorylation, these turtles are able to reduce their metabolic rate and recruit ...
Neal J Dawson   +2 more
doaj   +1 more source

A Rationally Designed Aldolase Foldamer [PDF]

open access: yesAngewandte Chemie, 2009
Current strategies for creating enzyme-like catalysts range from rational[1] and computational design[2] to evolutionary searches of large molecular libraries.[3] Sequence-specific polymers are particularly attractive starting points for these efforts because of their ability to adopt three-dimensional structures that preorganize functional groups for ...
Müller Manuel M   +4 more
openaire   +2 more sources

Structures, characteristics and functions of fructose-1,6-bisphosphate aldolase in various tissues

open access: yesActa Societatis Botanicorum Poloniae, 2023
Aldolase exhibits multiple functions in a variety of organisms, including fungi, unicellular algae and plants, and so on. Furthermore, different isoforms of fructose 1,6-bisphosphate aldolase (FBA) exhibit significantly different characteristics and ...
Lina Yang   +4 more
doaj   +1 more source

A deeply branching thermophilic bacterium with an ancient acetyl-CoA pathway dominates a subsurface ecosystem [PDF]

open access: yes, 2012
A nearly complete genome sequence of Candidatus ‘Acetothermum autotrophicum’, a presently uncultivated bacterium in candidate division OP1, was revealed by metagenomic analysis of a subsurface thermophilic microbial mat community.
A Stamatakis   +69 more
core   +8 more sources

A new intermediate of the aldolase reaction, the pyruvaldehyde-aldolase-orthophosphate complex [PDF]

open access: yesBiochemical Journal, 1978
Fructose 1,6-bisphosphate aldolase from rabbit muscle forms by reaction with dihydroxyacetone phosphate a pyruvaldehyde-aldolase-orthophosphate complex that is in equilibrium with the eneamine intermediate. The new intermediate accumulates in two phases.
E, Grazi, G, Trombetta
openaire   +2 more sources

LOXL2-dependent deacetylation of aldolase A induces metabolic reprogramming and tumor progression

open access: yesRedox Biology, 2022
Lysyl-oxidase like-2 (LOXL2) regulates extracellular matrix remodeling and promotes tumor invasion and metastasis. Altered metabolism is a core hallmark of cancer, however, it remains unclear whether and how LOXL2 contributes to tumor metabolism.
Ji-Wei Jiao   +15 more
doaj   +1 more source

Asymmetric Conjugate Hydrocyanation of α,β-Unsaturated Aldehydes Catalyzed by Engineered 2-Deoxy-D-ribose-5-phosphate Aldolase. [PDF]

open access: yesChemistry
The power of catalytic promiscuity: The enantioselective conjugate hydrocyanation of enals remains a long‐standing challenge for biocatalysis. Here, we report the redesign of 2‐deoxy‐D‐ribose‐5‐phosphate aldolase for the asymmetric conjugate hydrocyanation of aromatic enals, expanding the reaction scope of iminium‐based enzyme catalysis to include an ...
Zhou H, Fodran P, Fu H, Poelarends GJ.
europepmc   +2 more sources

Nuclear localization of aldolase A correlates with cell proliferation.

open access: yesBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2013
Muscle fructose 1,6-bisphosphate aldolase (ALDA) is a glycolytic enzyme which may localize both in nuclei and cytoplasm of cells, however its role in the nuclei is unclear. Here, we demonstrate the links between subcellular localization of ALDA and the cell cycle progression as well as the availability of energetic substrates.
P. Mamczur   +4 more
semanticscholar   +4 more sources

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