Results 341 to 350 of about 197,995 (383)

Metabolic and Epigenetic Control of CD8⁺ T Cell Exhaustion: The Acetate-to-Citrate Switch. [PDF]

MedComm (2020)
Lei X, Zhang W, Zhang D.
europepmc   +1 more source

Deciphering the structural consequences of R83 and R152 methylation on DNA polymerase β using molecular modeling. [PDF]

PLoS One
Srivastava A, Idriss H, Das G, Abedrabbo S, Shamsir MS, Homouz D.   +5 more
europepmc   +1 more source

17α-Hydroxylase/17,20-lyase Deficiency (17-OHD): A Meta-analysis of Reported Cases.

J Clin Endocrinol Metab
Willemsen AL, Torpy DJ, De Sousa SMC, Falhammar H, Rushworth RL.   +4 more
europepmc   +1 more source

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Polysaccharide lyases

Applied Biochemistry and Biotechnology, 1987
Polysaccharide lyases (or eliminases) are a class of enzymes (EC 4.2.2.-) that act to cleave certain activated glycosidic linkages present in acidic polysaccharides. These enzymes act through an eliminase mechanism, rather than through hydrolysis, resulting in unsaturated oligosaccharide products.
Robert J. Linhardt, Charles L. Cooney, P. M. Galliher   +2 more
openaire   +3 more sources

Adenylosuccinate lyase deficiency

Molecular Genetics and Metabolism, 2006
Adenylosuccinate lyase deficiency is a disease of purine metabolism which affects patients both biochemically and behaviorally. The symptoms are variable and include psychomotor retardation, autistic features, hypotonia, and seizures. Patients also accumulate the substrates of ADSL in body fluids.
David Patterson, David Patterson, Erin K. Spiegel, Erin K. Spiegel, Roberta F. Colman   +4 more
openaire   +2 more sources

Selenocysteine Lyase

EcoSal Plus, 2004
Selenocysteine is a naturally occurring analog of cysteine in which the sulfur atom of the latter is replaced with selenium. This seleno-amino acid occurs as a specific component of various selenoproteins and selenium-dependent enzymes.
openaire   +2 more sources

Structure and mechanism of tryptophan indole-lyase and tyrosine phenol-lyase

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2003
Tyrosine phenol-lyase (TPL) and tryptophan indole-lyase (Trpase) catalyse the reversible hydrolytic cleavage of L-tyrosine or L-tryptophan to phenol or indole, respectively, and ammonium pyruvate. These enzymes are very similar in sequence and structure, but show strict specificity for their respective physiological substrates.
Robert S. Phillips, Nicolai G. Faleev, Tatyana V. Demidkina   +2 more
openaire   +3 more sources

The first structure of pectate lyase belonging to polysaccharide lyase family 3

Acta Crystallographica Section D Biological Crystallography, 2001
The crystal structure of a highly alkaline low molecular weight pectate lyase (Pel-15) was determined at 1.5 A resolution by the multiple isomorphous replacement (MIR) method. This is the first pectate lyase structure from polysaccharide lyase family 3.
Atsuo Suzuki, Tohru Kobayashi, Susumu Ito, Takashi Yamane, Masatake Akita   +4 more
openaire   +3 more sources