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Targeting sphingosine-1-phosphate lyase as an anabolic therapy for bone loss

Nature Medicine, 2018
Jens W Fischer   +2 more
exaly   +2 more sources

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.
R J, Linhardt   +2 more
openaire   +2 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.
Erin K, Spiegel   +2 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   +2 more
openaire   +2 more sources

Pectate and Pectin Lyases

2002
In this chapter the differences and similarities between pectate lyases and pectin lyases are ...
Benen, J.A.E., Visser, J.
openaire   +2 more sources

Alginate Lyases of Pseudomonads*

The Journal of Biochemistry, 1969
Y, Kashiwabara, H, Suzuki, K, Nisizawa
openaire   +2 more sources

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