Use of site-directed chemical modification to study an essential lysine in Escherichia coli leader peptidase. (Q54567779)

1 June 2018

title

Use of site-directed chemical modification to study an essential lysine in Escherichia coli leader peptidase. (English)

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1 June 2018

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Paetzel M

1

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1 June 2018

Strynadka NC

2

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1 June 2018

Tschantz WR

3

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1 June 2018

Casareno R

4

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1 June 2018

Bullinger PR

5

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1 June 2018

Dalbey RE

6

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1 June 2018

language of work or name

English

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publication date

1 April 1997

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1 June 2018

Journal of Biological Chemistry

published in

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1 June 2018

volume

272

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1 June 2018

issue

15

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1 June 2018

page(s)

9994-10003

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1 June 2018

Isolation of the Escherichia coli leader peptidase gene and effects of leader peptidase overproduction in vivo

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Evidence that the catalytic activity of prokaryote leader peptidase depends upon the operation of a serine-lysine catalytic dyad

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Structure of the UmuD' protein and its regulation in response to DNA damage

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Families of serine peptidases.

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Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme

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Reengineering the catalytic lysine of aspartate aminotransferase by chemical elaboration of a genetically introduced cysteine

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Mechanism of the reaction catalyzed by acetoacetate decarboxylase. Importance of lysine 116 in determining the pKa of active-site lysine 115

21 January 2018

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Molecular structure of the acyl-enzyme intermediate in beta-lactam hydrolysis at 1.7 A resolution

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Construction of Biologically Functional Bacterial Plasmids In Vitro

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Examining the structural and chemical flexibility of the active site base, Lys-258, of Escherichia coli aspartate aminotransferase by replacement with unnatural amino acids

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Ribonuclease a: revealing structure-function relationships with semisynthesis

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Decreasing the basicity of the active site base, Lys-258, of Escherichia coli aspartate aminotransferase by replacement with gamma-thialysine

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A role for the epsilon-amino group of lysine-334 of ribulose-1,5-bisphosphate carboxylase in the addition of carbon dioxide to the 2,3-enediol(ate) of ribulose 1,5-bisphosphate.

21 January 2018

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Ellman's reagent: 5,5′-dithiobis(2-nitrobenzoic acid)—a reexamination

21 January 2018

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A general method applicable to the search for similarities in the amino acid sequence of two proteins

21 January 2018

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Raster3D Version 2.0. A program for photorealistic molecular graphics

21 January 2018

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Identification of the potential active site of the signal peptidase SipS of Bacillus subtilis. Structural and functional similarities with LexA-like proteases

21 January 2018

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On the role of methionine residues in the sequence-independent recognition of nonpolar protein surfaces

21 January 2018

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Leader Peptidase from Escherichia coli: Overexpression, Characterization, and Inactivation by Modification of Tryptophan Residues 300 and 310 with N-Bromosuccinimide1

21 January 2018

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Constrained multiple sequence alignment using XALIGN.

21 January 2018

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A New Synthetic Substrate for Trypsin and its Application to the Determination of the Amino-acid Sequence of Proteins

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.272.15.9994

1 reference

1 June 2018

release_nuicrt5vknanlmxax5rc65ksti

Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/nuicrt5vknanlmxax5rc65ksti

mapped directly with Wikidata item

24 November 2022

based on heuristic

1 reference

1 June 2018