Primary structure of Serratia marcescens anthranilate synthase component II.
TLDR
The amino acid sequence of anthranilate synthase component II (AS II) from Serratia marcescens was determined and the active site region is virtually identical to that of the Pseudomonas putida AS II enzyme.About:
This article is published in Journal of Biological Chemistry.The article was published on 1980-02-25 and is currently open access. It has received 37 citations till now. The article focuses on the topics: Anthranilate synthase & Serratia marcescens.read more
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A Metabolic Node in Action: Chorismate-Utilizing Enzymes in Microorganisms
TL;DR: Five chorismate-utilizing enzymes have been characterized in microorganisms in terms of the corresponding gene structures and regulation, nucleotide and protein sequences, protein structures, and reaction mechanisms, and the main emphasis is on transcriptional and posttranslational regulatory mechanisms.
Journal ArticleDOI
Characterization and derivation of the gene coding for mitochondrial carbamyl phosphate synthetase I of rat.
TL;DR: The protein sequence data provide strong evidence that the carbamyl phosphate synthetase I gene of rat, the carAB gene of E. coli, and the CPA1 and CPA2 genes of yeast were derived from common ancestral genes.
Journal ArticleDOI
Nucleotide sequence of Saccharomyces cerevisiae genes TRP2 and TRP3 encoding bifunctional anthranilate synthase:indole-3-glycerol phosphate synthase
TL;DR: Comparisons of TRP3 amino acid sequence with homologous sequences from E. coli and Neurospora crassa support the conclusion that the amino acids sequence of connectors in homologously multifunctional enzymes need not be conserved.
Journal ArticleDOI
The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, l-tryptophan
TL;DR: The crystal structure of anthranilate synthase from Serratia marcescens has been solved and reveals how occupancy of only one of the two feedback inhibition sites can immobilize the catalytic activity of both TrpE subunits.
Journal ArticleDOI
The rudimentary gene of Drosophila melanogaster encodes four enzymic functions
Jean-Noël Freund,B. P. Jarry +1 more
TL;DR: It is concluded that the rudimentary gene of Drosophila melanogaster encodes four enzymically different functions, each function restricted to a specific coding domain but in an order different from that previously defined by genetic data.
References
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The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis
Klaus Weber,Mary Osborn +1 more
TL;DR: The results show that the polyacrylamide gel electrophoresis method can be used with great confidence to determine the molecular weights of polypeptide chains for a wide variety of proteins.
Journal ArticleDOI
A Protein Sequenator
TL;DR: The protein sequenator is an instrument for the automatic determination of amino acid sequences in proteins and peptides that operates on the principle of the phenylisothiocyanate degradation scheme and has been applied to the whole molecule of apomyoglobin from the humpback whale.
Journal ArticleDOI
Rapid analysis of amino acid phenylthiohydantoins by high-performance liquid chromatography.
TL;DR: All 20 amino acid phenylthiohydantoins (PTHs) can be separated in a single analysis in less than 20 min using a 25 × 0.46-cm DuPont Zorbax ODS column and with this procedure it is possible to keep pace with automated Edman methods.
Book ChapterDOI
[20] Reduction and S-carboxymethylation of proteins
TL;DR: The extent to which complete reduction and S-carboxymethylation have been attained is determined by amino acid analysis and serves as a check on the extent of side reactions such as sulfonium salt or sulfoxide formation from methionine and modification of histidine or lysine.