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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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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 Ī²-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 Ī²-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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Biochemistry, 2018
Marine organisms release dimethylsulfide (DMS) via cleavage of dimethylsulfoniopropionate (DMSP). Different genes encoding proteins with DMSP lyase activity are known, yet these exhibit highly variable levels of activity.
L. Lei +4 more
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Marine organisms release dimethylsulfide (DMS) via cleavage of dimethylsulfoniopropionate (DMSP). Different genes encoding proteins with DMSP lyase activity are known, yet these exhibit highly variable levels of activity.
L. Lei +4 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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On the Mechanism of Action of Isocitrate Lyase
European Journal of Biochemistry, 1975The enzymes citrate lyase and isocitrate lyase catalyse similar reactions in the cleavage of citrate to acetate plus oxaloacetate and of isocitrate to succinate plus glyoxylate, respectively. Nevertheless, the mechanism of action of each enzyme appears to be different from each other. Citrate lyase is an acyl carrier proteinācontaining enzyme complex
Klaus K. Mayer +2 more
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Role of bifunctional ammonia-lyase in grass cell wall biosynthesis
Nature Plants, 2016J. Barros +5 more
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