Results 181 to 190 of about 3,470 (215)
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Histidine ammonia-lyase from Streptomyces griseus
Gene, 1992Histidine ammonia-lyase (histidase; HutH) has been purified to homogeneity from Streptomyces griseus and the N-terminal amino acid (aa) sequence used to clone the histidase-encoding structural gene, hutH. The purified enzyme shows typical saturation kinetics and is inhibited competitively by D-histidine and histidinol phosphate.
P C, Wu +3 more
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Phenylalanine ammonia-lyase gene organization and structure
Plant Molecular Biology, 1989Phenylalanine ammonia-lyase (PAL; EC 4.3.1.5) genomic sequences were isolated from bean (Phaseolus vulgaris L.) genomic libraries using elicitor-induced bean PAL cDNA sequences as a probe. Southern blot hybridization of genomic DNA fragments revealed three divergent classes of PAL genes in the bean genome.
C L, Cramer +8 more
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A modern view of phenylalanine ammonia lyase
Biochemistry and Cell Biology, 2007Phenylalanine ammonia lyase (PAL; E.C.4.3.1.5), which catalyses the biotransformation of l-phenylalanine to trans-cinnamic acid and ammonia, was first described in 1961 by Koukol and Conn. Since its discovery, much knowledge has been gathered with reference to the enzyme’s catabolic role in microorganisms and its importance in the phenyl propanoid ...
M Jason, MacDonald, Godwin B, D'Cunha
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Journal of Plant Physiology, 2003
Phenylalanine ammonia-lyase (PAL, EC 4.3.1.5) and tyrosine ammonia-lyase (TAL, 4.3.1.), the key enzymes of the phenylpropanoid pathway, are inducible in response to biotic (such as chitin from fungal cell walls) and abiotic cues. Application of chitin and chitosan to soybean leaf tissues caused increased activity of PAL and TAL enzymes.
Wajahatullah, Khan +2 more
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Phenylalanine ammonia-lyase (PAL, EC 4.3.1.5) and tyrosine ammonia-lyase (TAL, 4.3.1.), the key enzymes of the phenylpropanoid pathway, are inducible in response to biotic (such as chitin from fungal cell walls) and abiotic cues. Application of chitin and chitosan to soybean leaf tissues caused increased activity of PAL and TAL enzymes.
Wajahatullah, Khan +2 more
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[149a] Histidine ammonia-lyase (Pseudomonas)
1971Publisher Summary This chapter focuses on Histidine Ammonia-Lyas (Pseudomonas). Histidine ammonia-lyase is assayed spectrophotometrically. At 277 mμ, urocanate has an extinction coefficient of 1.88 × l0 4 M -1 cm -1 . The enzymatic conversion of L -histidine to urocanate has been considered irreversible— 15 NH 3 added to the reaction mixture does
Matthew M. Reghler, Herbert Tabor
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Properties of yeast l-phenylalanine ammonia-lyase
Archives of Biochemistry and Biophysics, 1972Abstract l -Phenylalanine ammonia-lyase from the yeast Rhodotorula glutinis is inhibited by the halide anions iodide, bromide, and chloride. Iodide acts as a competitive inhibitor of phenylalanine deamination. The enzyme is deactivated by reagents attacking either amino or sulfhydryl functional groups and contains approximately two catalytically ...
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Diaminopropionate Ammonia-Lyase Of Salmonella Typhimurium
1987Remarkable activity of 2,3-diaminopropionate(DAP) ammonia-lyase was found in Salmonella typhimurium. The emzyme was purified and crystallized from S. typhimurium. The relative molecular mass of the native enzyme, estimated by the ultracentrifugal equilibrium method, is 89000Da, and the enzyme consists of two subunits identical in molecular mass.
T. Nagasawa +3 more
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[149b] Histidine ammonia-lyase (Pseudomonas)
1971Publisher Summary This chapter focuses on Histidine Ammonia-Lyase ( Pseudomonas ). Histidine ammonia-lyase from Pseudomonas is found to exist as a mixture of enzymatically active polymeric species held together by disulfide cross links. Each of the isolated monomeric and polymeric species is active without added thiols. Treatment with thiols, however,
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