Circular permutation analysis as a method for distinction of functional elements in the M20 loop of Escherichia coli dihydrofolate reductase (Q77926887)

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scientific article published on 01 July 1999

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English	Circular permutation analysis as a method for distinction of functional elements in the M20 loop of Escherichia coli dihydrofolate reductase	scientific article published on 01 July 1999

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scholarly article

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10383405%20AND%20SRC:MED&resulttype=core&format=json

9 December 2019

Circular permutation analysis as a method for distinction of functional elements in the M20 loop of Escherichia coli dihydrofolate reductase (English)

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9 December 2019

Escherichia coli

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Tsutomu Nakamura

1

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9 December 2019

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M Iwakura

2

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9 December 2019

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1 July 1999

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9 December 2019

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7

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Journal of Biological Chemistry

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9 December 2019

274

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9 December 2019

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9 December 2019

19041-19047

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9 December 2019

Deletion of a highly motional residue affects formation of the Michaelis complex for Escherichia coli dihydrofolate reductase

1 reference

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Strength of an interloop hydrogen bond determines the kinetic pathway in catalysis by Escherichia coli dihydrofolate reductase

1 reference

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Correct folding of circularly permuted variants of a beta alpha barrel enzyme in vivo

1 reference

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21 January 2018

A fully active variant of dihydrofolate reductase with a circularly permuted sequence.

1 reference

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Circularly permuted dihydrofolate reductase of E. coli has functional activity and a destabilized tertiary structure.

1 reference

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Effects of the length of a glycine linker connecting the N-and C-termini of a circularly permuted dihydrofolate reductase.

1 reference

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Aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains

1 reference

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Random circular permutation of genes and expressed polypeptide chains: application of the method to the catalytic chains of aspartate transcarbamoylase

1 reference

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Permuteins of interleukin 1 beta--a simplified approach for the construction of permutated proteins having new termini

1 reference

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Circular permutation of T4 lysozyme

1 reference

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Native-like in vivo folding of a circularly permuted jellyroll protein shown by crystal structure analysis

1 reference

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The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics

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A circularly permuted recombinant interleukin 4 toxin with increased activity

1 reference

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Circular permutation within the coenzyme binding domain of the tetrameric glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus.

1 reference

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Kinetics of translation of gamma B crystallin and its circularly permutated variant in an in vitro cell-free system: possible relations to codon distribution and protein folding

1 reference

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High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis

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Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate.NADP+ ternary complex. Substrate binding and a model for the transition state

1 reference

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21 January 2018

Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding

1 reference

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Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence

1 reference

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21 January 2018

Functional role of a mobile loop of Escherichia coli dihydrofolate reductase in transition-state stabilization

1 reference

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Dynamics of a flexible loop in dihydrofolate reductase from Escherichia coli and its implication for catalysis.

1 reference

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21 January 2018

Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli

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Dihydrofolate Reductase as a New “Affinity Handle”

1 reference

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21 January 2018

Folding of dihydrofolate reductase from Escherichia coli.

1 reference

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21 January 2018

Kinetic mechanism of the reaction catalyzed by dihydrofolate reductase from Escherichia coli.

1 reference

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21 January 2018

Mechanism of the reaction catalyzed by dihydrofolate reductase from Escherichia coli: pH and deuterium isotope effects with NADPH as the variable substrate

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Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants

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A Strategy for Testing the Suitability of Cysteine Replacements in Dihydrofolate Reductase from Escherichia coli1

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Effects of point mutations at the flexible loop alanine-145 of Escherichia coli dihydrofolate reductase on its stability and function

1 reference

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Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid

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Enzyme Mechanisms, Models, and Mimics

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Correlation of DNA exonic regions with protein structural units in haemoglobin

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Modular structural units, exons, and function in chicken lysozyme

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Assembly of a class I tRNA synthetase from products of an artificially split gene.

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Stable substructures of eightfold beta alpha-barrel proteins: fragment complementation of phosphoribosylanthranilate isomerase

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Identifiers

10.1074/JBC.274.27.19041

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10383405%20AND%20SRC:MED&resulttype=core&format=json

9 December 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10383405%20AND%20SRC:MED&resulttype=core&format=json

9 December 2019

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