Organization of enzymes in the polyaromatic synthetic pathway: separability in bacteria.
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The purification of shikimate dehydrogenase from Escherichia coliSequencing and overexpression of the Escherichia coli aroE gene encoding shikimate dehydrogenaseIsolation of the ARO1 cluster gene of Saccharomyces cerevisiae.Implications of some genetic control mechanisms in NeurosporaOrganization of polyaromatic biosynthetic enzymes in a variety of photosynthetic organismsAdvances in Streptomyces coelicolor geneticsExpression in Escherichia coli K-12 of the structural gene for catabolic dehydroquinase of Neurospora crassa.Unusual ancestry of dehydratases associated with quinate catabolism in Acinetobacter calcoaceticusRepression of aromatic amino acid biosynthesis in Escherichia coli K-12Organization of enzymes in the common aromatic synthetic pathway: evidence for aggregation in fungi.The aromatic amino acid pathway branches at L-arogenate in Euglena gracilisInfluence of an aggregated multienzyme system on transient time: kinetic evidence for compartmentation by an aromatic-amino-acid synthesizing complex of Neurospora crassaPartial enzyme aggregates formed by pleiotropic mutants in the arom gene cluster of Neurospora crassaConstitutive and repressivle enzymes of the common pathway of aromatic biosynthesis in Escherichia coli K-12: regulation of enzyme synthesis at different growth rates.Identification of the gene (aroK) encoding shikimic acid kinase I of Escherichia coli.Genetic and molecular analysis of aroL, the gene for shikimate kinase II in Escherichia coli K-12.Aromatic amino acid biosynthesis: regulation of shikimate kinase in Escherichia coli K-12.The pentafunctional arom enzyme of Saccharomyces cerevisiae is a mosaic of monofunctional domains.Purification and characterization of 3-dehydroquinase from Escherichia coli.Efficient independent activity of a monomeric, monofunctional dehydroquinate synthase derived from the N-terminus of the pentafunctional AROM protein of Aspergillus nidulansIdentification of the active-site lysine residues of two biosynthetic 3-dehydroquinases.The serC-aro A operon of Escherichia coli. A mixed function operon encoding enzymes from two different amino acid biosynthetic pathways.The 3-dehydroquinate synthase activity of the pentafunctional arom enzyme complex of Neurospora crassa is Zn2+-dependent.Isolation of a bifunctional domain from the pentafunctional arom enzyme complex of Neurospora crassaThe purification and characterization of 3-dehydroquinase from Streptomyces coelicolor.The cloning and expression of the aroL gene from Escherichia coli K12. Purification and complete amino acid sequence of shikimate kinase II, the aroL-gene product.The overexpression and complete amino acid sequence of Escherichia coli 3-dehydroquinase.Purification of 5-enolpyruvylshikimate 3-phosphate synthase from Escherichia coli.
P2860
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P2860
Organization of enzymes in the polyaromatic synthetic pathway: separability in bacteria.
description
1969 nî lūn-bûn
@nan
1969年の論文
@ja
1969年論文
@yue
1969年論文
@zh-hant
1969年論文
@zh-hk
1969年論文
@zh-mo
1969年論文
@zh-tw
1969年论文
@wuu
1969年论文
@zh
1969年论文
@zh-cn
name
Organization of enzymes in the polyaromatic synthetic pathway: separability in bacteria.
@ast
Organization of enzymes in the polyaromatic synthetic pathway: separability in bacteria.
@en
type
label
Organization of enzymes in the polyaromatic synthetic pathway: separability in bacteria.
@ast
Organization of enzymes in the polyaromatic synthetic pathway: separability in bacteria.
@en
prefLabel
Organization of enzymes in the polyaromatic synthetic pathway: separability in bacteria.
@ast
Organization of enzymes in the polyaromatic synthetic pathway: separability in bacteria.
@en
P2860
P1476
Organization of enzymes in the polyaromatic synthetic pathway: separability in bacteria.
@en
P2093
P2860
P304
P407
P577
1969-07-01T00:00:00Z