Results 31 to 40 of about 10,567,748 (150)

A methylaspartate cycle in haloarchaea

open access: yes, 2011
Access to novel ecological niches often requires adaptation of metabolic pathways to cope with new environments. For conversion to cellular building blocks, many substrates enter central carbon metabolism via acetyl-coenzyme A (acetyl-CoA).
Thomas, L.   +4 more
core   +1 more source

The Role of Reticulate Evolution in Creating Innovation and Complexity

open access: yesInternational Journal of Evolutionary Biology, Volume 2012, Issue 1, 2012., 2012
Reticulate evolution encompasses processes that conflict with traditional Tree of Life efforts. These processes, horizontal gene transfer (HGT), gene and whole‐genome duplications through allopolyploidization, are some of the main driving forces for generating innovation and complexity. HGT has a profound impact on prokaryotic and eukaryotic evolution.
Kristen S. Swithers   +3 more
wiley   +1 more source

Nitric oxide delays the postharvest nutritional quality decline of “Golden Hook” beans

open access: yesFood Frontiers, Volume 5, Issue 2, Page 636-655, March 2024.
NO treatment can enhance the defense ability of “Golden Hook” beans by enhancing the expression of resistance gene and promoting the expression of jasmonic acid defense pathway. NO also induced the biosynthesis of flavonoids and the accumulation of related metabolites by regulating the expression of antioxidant enzyme genes, thus enhancing its ...
Xuelian He   +10 more
wiley   +1 more source

Biocatalytic Enantioselective Hydroaminations for Production of N-Cycloalkyl-Substituted L-Aspartic Acids Using Two C-N Lyases [PDF]

open access: yes, 2019
N‐cycloalkyl‐substituted amino acids have wide‐ranging applications in pharma‐ and nutraceutical fields. Here we report the asymmetric synthesis of various N‐cycloalkyl‐substituted L‐aspartic acids using ethylenediamine‐N,N'‐disuccinic acid lyase (EDDS ...
Tepper, Pieter   +8 more
core   +1 more source

Malate Synthase and β-Methylmalyl Coenzyme A Lyase Reactions in the Methylaspartate Cycle in Haloarcula hispanica

open access: yes, 2017
Haloarchaea are extremely halophilic heterotrophic microorganisms belonging to the class Halobacteria (Euryarchaeota). Almost half of the haloarchaea possesses the genes coding for enzymes of the methylaspartate cycle, a recently discovered anaplerotic ...
Xiang, H.   +5 more
core   +1 more source

Interconversion of (S)-Glutamate and (2S,3S)-3-Methylaspartate:  A Distinctive B12-Dependent Carbon-Skeleton Rearrangement

open access: yes, 2016
The interconversion of (S)-glutamate and (2S,3S)-3-methylaspartate catalyzed by B12-dependent glutamate mutase is discussed using results from high-level ab initio molecular orbital calculations.
Stacey D. Wetmore (696456)   +3 more
core   +1 more source

Research progress of gene target therapy for refractory epilepsy

open access: yesChinese Journal of Contemporary Neurology and Neurosurgery, 2014
Nowadays, the strategies of gene therapy for the treatment of refractory epilepsy (RE) mainly include modulating neurotransmitter systems, neuropeptide Y (NPY) and neurotrophic factors.
Xing-hua TANG, Lin LI, Zhen-guo LIU
doaj  

Characterization and biocatalytic applications of aspartate and methylaspartate ammonia lyases [PDF]

open access: yes, 2012
In zijn promotieonderzoek heeft Vinod Puthan Veetil het katalytische mechanisme van aspartaat ammonia lyase, dat lange tijd onbekend was, opgehelderd. Ook heeft hij het biokatalytische potentieel van een variant van methylaspartaat ammonia lyase benut ...
Puthan Veetil, Vinod,   +1 more
core  

Resolución CSPyGE N° 28/2022. Derogar las Resoluciones CSPyGE N° 14/2022 y N° 15/2020. Convalidar la Resolución Rectoral N° 825/2022.

open access: yes, 2022
Fil: Consejo Superior de Programación y Gestión Estratégica (P). Universidad Nacional de Río Negro. Río Negro, ArgentinaResolución CSPyGE N° 28/2022. Derogar las Resoluciones CSPyGE N° 14/2022 y N° 15/2020.
Consejo Superior de Programación y Gestión Estratégica (P)
core  

Mechanistic studies of the enzyme 3-methylaspartate ammonia-lyase

open access: yes, 1989
3-Methylaspartate ammonia-lyase (E.C. 4.3.1.2), catalyses the reversible elimination of ammonia from methylaspartic acid. The enzyme from Clostridium tetanomorphum has been purified to homogeneity in three stages using a new method; acetone fractionation
Cohen, Mark Adam
core  

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