Evidence that mutations in a loop region of the alpha-subunit inhibit the transition from an open to a closed conformation in the tryptophan synthase bienzyme complex.

Evidence that mutations in a loop region of the alpha-subunit inhibit the transition from an open to a closed conformation in the tryptophan synthase bienzyme complex.

Item
http://www.wikidata.org/entity/Q30195343
Allostery and Substrate Channeling in the Tryptophan Synthase Bienzyme Complex: Evidence for Two Subunit Conformations and Four Quaternary StatesSevering of a hydrogen bond disrupts amino acid networks in the catalytically active state of the alpha subunit of tryptophan synthase.NMR crystallography of enzyme active sites: probing chemically detailed, three-dimensional structure in tryptophan synthaseThe Dsl1 tethering complex actively participates in soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor (SNARE) complex assembly at the endoplasmic reticulum in Saccharomyces cerevisiae.Visualizing the tunnel in tryptophan synthase with crystallography: Insights into a selective filter for accommodating indole and rejecting waterThe tryptophan synthase α2β2 complex: a model for substrate channeling, allosteric communication, and pyridoxal phosphate catalysis.Gates of enzymes.Allosteric regulation of substrate channeling and catalysis in the tryptophan synthase bienzyme complex.The stereospecificity and catalytic efficiency of the tryptophan synthase-catalysed exchange of the alpha-protons of amino acidsThe functional role of a conserved loop in EAL domain-based cyclic di-GMP-specific phosphodiesterase.Tryptophan synthase: structure and function of the monovalent cation site.Factors affecting the stereospecificity and catalytic efficiency of the tryptophan synthase-catalysed exchange of the pro-2R and pro-2S protons of glycine
P2860

Evidence that mutations in a loop region of the alpha-subunit inhibit the transition from an open to a closed conformation in the tryptophan synthase bienzyme complex.

Item
http://www.wikidata.org/entity/Q30195343
description
1992 nî lūn-bûn
@nan
1992 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Evidence that mutations in a l ...... han synthase bienzyme complex.
@ast
Evidence that mutations in a l ...... han synthase bienzyme complex.
@en
type
label
Evidence that mutations in a l ...... han synthase bienzyme complex.
@ast
Evidence that mutations in a l ...... han synthase bienzyme complex.
@en
prefLabel
Evidence that mutations in a l ...... han synthase bienzyme complex.
@ast
Evidence that mutations in a l ...... han synthase bienzyme complex.
@en
P1433
P1476
P2093
P304
P31
P407
P433
P478
P577
P698
P1433
P1476
Evidence that mutations in a l ...... han synthase bienzyme complex.
@en
P2093
P304
P31
P407
P433
P478
P577
P698