Partial purification and properties of tryptophan synthase of pea (Pisum sativum L.) plants
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Partial purification and properties of tryptophan synthase of pea (Pisum sativum L.) plants

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Published .
Written in English


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Book details:

Edition Notes

Other titlesTryptophan synthase.
Statementby Ronald Tsutomu Nagao.
The Physical Object
Pagination[14], 97 leaves, bound :
Number of Pages97
ID Numbers
Open LibraryOL14242978M

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Tryptophan and its analogues induced the de novo synthesis of the initial enzyme of the alkaloid biosynthesis, dimethylallyl tryptophan synthase. Tryptophan induces the synthesis of another enzyme of the pathway, namely, chanoclavine cyclase. Methionine plays an inductive role in the fosfomycin biosynthesis by Streptomyces fradiae. May 17,  · The aromatic amino acids phenylalanine, tyrosine and tryptophan in plants are not only essential components of protein synthesis, but also serve as precursors for a wide range of secondary metabolites that are important for plant growth as well as for human nutrition and by: Abstract. The field of amino acid biosynthesis from inorganic nitrogen has been one of the most active in plant biochemistry in the last five years and a recent book has been devoted entirely to it (M iflin a). To provide a reasonable coverage of the field in a short chapter is difficult; here we present an outline of the biochemical pathways involved in the flow of nitrogen from ammonia Cited by: Mar 01,  · Mutations at the rug5 (rug osus 5) locus have been used to elucidate the role of the major soluble isoform of starch synthase II (SSII) in amylopectin synthesis in the developing pea embryo. The SSII gene maps to the rug5 locus, and the gene in one of three rug5 mutant lines has been shown to carry a base pair substitution that introduces a stop codon into the open reading by:

Anthranilate synthetase, which is normally feedback inhibited by l-tryptophan, was much more sensitive to inhibition by all the analogs than was tryptophan synthetase Purification and properties of Salmonella typhimurium acetolactate synthase isozyme II from Escherichia coli HB/pDU9. Biochemistry , 24 (18), DOI: /bia Rolf Braenden, Thomas Nilsson, and Stenbjoern by: Apr 13,  · Compared with normal subjects, low tryptophan and a low ratio of tryptophan to other amino acids were seen in the obese study subjects throughout the hour period The significance of this low ratio of tryptophan is that the other amino acids compete with tryptophan for transport through the blood-brain barrier. Tyrosine—tRNA ligase (EC ), also known as tyrosyl-tRNA synthetase (symbol YARS), is an enzyme that catalyzes the chemical reaction. ATP + L-tyrosine + tRNA(Tyr) ⇌ AMP + diphosphate + L-tyrosyl-tRNA(Tyr) The three substrates of this enzyme are ATP, L-tyrosine, and a tyrosine-specific transfer RNA [tRNA(Tyr) or tRNA Tyr], whereas its three products are AMP, diphosphate, and L BRENDA: BRENDA entry.

Plant Physiology: (3) Jul UPDATES Partial Purification of a cis-trans-Isomerase of Zeatin from Immature Seed of Phaseolus vulgaris L. N. V. Bassil, DWS. Expression Patterns of Duplicate Tryptophan Synthase [beta] Genes in Arabidopsis thaliana. K. D. Pruitt, R. L. Lithium and chlorimipramine differentially alter the stability properties of tryptophan hydroxylase as seen in allosteric and scattering kinetics Kinetik der Hexulosephosphat-Synthase methylotropher Bakterien in vitro und in situ Studies on nucleotide pyrophosphatase I. Partial purification and properties of a sheep liver enzyme that Cited by: Jun 14,  · Thus, we think that AtPGDH1 is responsible for the supply of serine as a substrate for tryptophan synthase (Fig. 10). In fact, tryptophan-derived metabolites such as Cited by: 8. May 01,  · Camptothecin is an anticancer drug produced by the monoterpene indole alkaloid pathway in Camptotheca acuminata. As part of an investigation of the camptothecin biosynthetic pathway, we have cloned and characterized a gene from C. acuminata encoding the β-subunit of tryptophan (Trp) synthase (TSB). In C. acuminata TSB provides Trp for both protein synthesis and Cited by: