Results 21 to 30 of about 9,258 (171)

Reversed argininosuccinate lyase activity in fumarate hydratase-deficient cancer cells. [PDF]

open access: yes, 2013
BACKGROUND: Loss of function of fumarate hydratase (FH), the mitochondrial tumor suppressor and tricarboxylic acid (TCA) cycle enzyme, is associated with a highly malignant form of papillary and collecting duct renal cell cancer.
Blyth, Karen   +9 more
core   +4 more sources

Discovery of novel highly active and stable aspartate dehydrogenases

open access: yesScientific Reports, 2017
Aspartate family amino acids (AFAAs) have important commercial values due to their wide spectrum of applications. Most if not all AFAAs are produced under aerobic conditions which is energy-intensive.
Hao Li   +6 more
doaj   +1 more source

Discovering functional gene expression patterns in the metabolic network of with wavelets transforms [PDF]

open access: yes, 2006
Background Microarray technology produces gene expression data on a genomic scale for an endless variety of organisms and conditions. However, this vast amount of information needs to be extracted in a reasonable way and funneled into manageable and ...
Zapatka Marc   +7 more
core   +2 more sources

Optimization of aspartate ammonia lyase production by Bacillus cereus

open access: yesJournal of Industrial Microbiology and Biotechnology, 2000
In an attempt to clarify the function of l-aspartic acid and culture conditions in aspartate ammonia lyase induction, experiments were carried out on aspartase formation in Bacillus cereus cells. The enzyme was produced by microorganisms in response to l-aspartic acid, which is catabolized by direct deamination to fumarate.
Y G Garza   +3 more
openaire   +1 more source

Synthesis of 3‐arsonoalanine and its action on aspartate aminotransferase and aspartate ammonia‐lyase [PDF]

open access: yesEuropean Journal of Biochemistry, 1993
dl‐3‐Arsonoalanine has been synthesized by the Strecker synthesis from the unstable compound arsonoacetaldehyde. It inactivates pig heart cytosolic aspartate aminotransferase and inhibits aspartate ammonia‐lyase by competing with aspartate (Ki/Km 0.23).
B R, Ali, H B, Dixon
openaire   +2 more sources

Hyperammonemia due to urea cycle disorders: a potentially fatal condition in the intensive care setting [PDF]

open access: yes, 2014
Disorders of the urea cycle are secondary to a defect in the system that converts ammonia into urea, resulting in accumulation of ammonia and other products. This results in encephalopathy, coma, and death if not recognized and treated rapidly.
Fabiano Pinheiro da Silva   +1 more
core   +1 more source

Effects of yellow seed coat mutation on oil and protein contents in seeds of Brassica napus L

open access: yes浙江大学学报. 农业与生命科学版, 2017
Seed coat colour was one of the most important agronomic traits in Brassica napus L., which was believed to be related with oil content and meal quality.
LIU Yu, WANG Fulin, LIU Renhu
doaj   +1 more source

Ammonia toxicity to the brain and creatine. [PDF]

open access: yes, 2004
Symptoms of hyperammonemia are age-dependent and some are reversible. Multiple mechanisms are involved. Hyperammonemia increases the uptake of tryptophan into the brain by activation of the L-system carrier while brain glutamine plays a still undefined ...
Bachmann, C.   +4 more
core   +1 more source

Metabolic network analysis reveals microbial community interactions in anammox granules. [PDF]

open access: yes, 2017
Microbial communities mediating anaerobic ammonium oxidation (anammox) represent one of the most energy-efficient environmental biotechnologies for nitrogen removal from wastewater.
Bhattacharjee, Ananda S   +6 more
core   +2 more sources

Site‐directed mutagenesis, kinetic and inhibition studies of aspartate ammonia lyase from Bacillus sp. YM55‐1 [PDF]

open access: yesThe FEBS Journal, 2009
Aspartate ammonia lyases (also referred to as aspartases) catalyze the reversible deamination of l‐aspartate to yield fumarate and ammonia. In the proposed mechanism for these enzymes, an active site base abstracts a proton from C3 of l‐aspartate to form an enzyme‐stabilized enediolate intermediate.
Veetil, Vinod Puthan   +4 more
openaire   +2 more sources

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