Results 231 to 240 of about 21,937 (291)

Molecular Characterization of a Novel Alkaline Endo-Pectate Lyase from <i>Paenibacillus borealis</i> and Over-Production in Bioreactor Realized by Constructing the Tandem Expression Cassettes in Host Genome. [PDF]

Molecules
Han Y, Peng XB, Wei SY, Chen QG, Yang JK.   +4 more
europepmc   +1 more source

Fecal Material of Captive Wild Animals as Source of CAZymes With Application Potential. [PDF]

Chembiochem
Bechtner J, Hosek J, Schwab C.
europepmc   +1 more source

Electrostatic tuning of the pyridoxal-5'-phosphate cofactor site defines pH dependence in type I cystathionine β-lyases. [PDF]

J Biol Chem
Liu Y, Li X, Li J, Liu J, Peng Y, Gao Y, Zhang Y, Jia Z, Kang K, Yin A, Ma C, Yang Y, Yang C.   +12 more
europepmc   +1 more source

A novel Flavobacterium quisquiliarum porphyrin binding protein independently disrupts Pseudomonas aeruginosa biofilms

Lelenaite I, Fletcher CS, Houppy W, Morley C, Brown A, Black GW, Malekpour AK, Brown NL, Singh W, Munoz J, Yau HCL, Lant NJ, Willats WGT.   +12 more
europepmc   +1 more source

Immobilisation of hydroxynitrile lyases

Chemical Society Reviews, 2013
Hydroxynitrile lyases are a versatile group of enzymes that are applied both in the laboratory and on an industrial scale. What makes them particularly interesting is that to date five structurally unrelated categories of hydroxynitrile lyases have been discovered.
Ulf Hanefeld
exaly   +8 more sources

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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.
R J, Linhardt, P M, Galliher, C L, Cooney   +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, Roberta F, Colman, David, Patterson   +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, Tatyana V, Demidkina, Nicolai G, Faleev   +2 more
openaire   +2 more sources