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Structure and mechanism of tryptophan indole-lyase and tyrosine phenol-lyase
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2003Tyrosine 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
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Spatial structure and the mechanism of tyrosine phenol-lyase and tryptophan indole-lyase
Molecular Biology, 2009The bacterial tyrosine phenol-lyase (EC 4.1.99.2) and tryptoptophan indole-lyase (EC 4.1.99.1) belong to pyridoxal-5'-phosphate dependent beta-eliminating lyases, catalysing the reversible decomposition of L-tyrosine and L-tryptophan to pyruvate, ammonia, and phenol or indole correspondingly.
L. N. Zakomirdina +4 more
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The first structure of pectate lyase belonging to polysaccharide lyase family 3
Acta Crystallographica Section D Biological Crystallography, 2001The 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 +4 more
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International Journal of Biological Macromolecules, 2011
A typical filamentous bacterium, Sphaerotilus natans, secretes a thiolic glycoconjugate which is assembled into a microtube, so called sheath. The glycoconjugate is known to consist of a pentasaccharide-dipeptide repeating unit, but its chemical structure has not been completely elucidated.
Mina Yamada +8 more
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A typical filamentous bacterium, Sphaerotilus natans, secretes a thiolic glycoconjugate which is assembled into a microtube, so called sheath. The glycoconjugate is known to consist of a pentasaccharide-dipeptide repeating unit, but its chemical structure has not been completely elucidated.
Mina Yamada +8 more
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2002
In this chapter the differences and similarities between pectate lyases and pectin lyases are ...
Benen, J.A.E., Visser, J.
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In this chapter the differences and similarities between pectate lyases and pectin lyases are ...
Benen, J.A.E., Visser, J.
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Cysteine conjugate beta-lyase.
Molecular Pharmacology, 1983Cysteine conjugate beta-lyase from rat liver, an enzyme participating in a shunt from mercapturic acid synthesis, has been purified and found to be active with a number of compounds that bear nonpolar leaving groups on the beta-carbon of an amino acid substrate. Pyridoxal phosphate is considered to be a participant in the reaction.
William B. Jakoby, James L. Stevens
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2017
Polysaccharide lyases are a diverse group of enzymes that degrade uronic acid-containing polysaccharides via a β-elimination mechanism. They are produced by a variety of organisms belonging to various domains of life such as bacteria, fungi, and marine animals.
A. Goyal +3 more
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Polysaccharide lyases are a diverse group of enzymes that degrade uronic acid-containing polysaccharides via a β-elimination mechanism. They are produced by a variety of organisms belonging to various domains of life such as bacteria, fungi, and marine animals.
A. Goyal +3 more
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Analysis of Glycosaminoglycans with Polysaccharide Lyases
Current Protocols in Molecular Biology, 1999Polysaccharide lyases are a class of enzymes useful for analysis of glycosaminoglycans (GAGs) and the glycosaminoglycan component of proteoglycans (PGs). These enzymes cleave specific glycosidic linkages present in acidic polysaccharides and result in depolymerization.
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1985
Publisher Summary This chapter provides an overview of aspartate ammonia-lyase, which catalyzes the reversible conversion of L-aspartic acid to fumarate and ammonia. Enzyme synthesis in Escherichia coli W cells is subject to catabolite repression by glucose and is suppressed under aerobic conditions.
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Publisher Summary This chapter provides an overview of aspartate ammonia-lyase, which catalyzes the reversible conversion of L-aspartic acid to fumarate and ammonia. Enzyme synthesis in Escherichia coli W cells is subject to catabolite repression by glucose and is suppressed under aerobic conditions.
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Phytochemistry, 1973
Abstract The literature concerning the physiology and biochemistry of the enzyme phenylalanine ammonia lyase (PAL) (E.C. 4.1.1.5) from different organisms has been reviewed. Levels of the enzyme are affected by age, light, phytochrome, wounding, infection and growth modifiers. The possibility that PAL is involved in the control of phenolic metabolism
Edith L. Camm, G.H.Neil Towers
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Abstract The literature concerning the physiology and biochemistry of the enzyme phenylalanine ammonia lyase (PAL) (E.C. 4.1.1.5) from different organisms has been reviewed. Levels of the enzyme are affected by age, light, phytochrome, wounding, infection and growth modifiers. The possibility that PAL is involved in the control of phenolic metabolism
Edith L. Camm, G.H.Neil Towers
openaire +2 more sources