Identification of the catalytic triad in tripeptidyl-peptidase II through site-directed mutagenesis (Q44225064)

1 December 2017

title

Identification of the catalytic triad in tripeptidyl-peptidase II through site-directed mutagenesis (English)

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1 December 2017

Hubert Hilbi

1

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1 December 2017

Emese Jozsa

series ordinal

2

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1 December 2017

Birgitta Tomkinson

series ordinal

3

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1 December 2017

publication date

1 December 2002

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1 December 2017

number of pages

6

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Biochimica et Biophysica Acta

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published in

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1 December 2017

volume

1601

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1 December 2017

issue

2

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1 December 2017

page(s)

149-154

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describes a project that uses

1 December 2017

site-directed mutagenesis

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Tripeptidyl peptidase II in haemolysates and liver homogenates of various species

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cites work

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7 January 2021

Characterization and cloning of tripeptidyl peptidase II from the fruit fly, Drosophila melanogaster

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7 January 2021

Tripeptidyl peptidases: enzymes that count

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7 January 2021

Integration of the ubiquitin-proteasome pathway with a cytosolic oligopeptidase activity

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7 January 2021

Characterization and inhibition of a cholecystokinin-inactivating serine peptidase

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7 January 2021

Tripeptidyl peptidase II promotes maturation of caspase-1 in Shigella flexneri-induced macrophage apoptosis

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7 January 2021

Supramolecular structure of tripeptidyl peptidase II from human erythrocytes as studied by electron microscopy, and its correlation to enzyme activity

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7 January 2021

A giant protease with potential to substitute for some functions of the proteasome

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7 January 2021

Active site of tripeptidyl peptidase II from human erythrocytes is of the subtilisin type

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7 January 2021

Characterization of cDNA for human tripeptidyl peptidase II: the N-terminal part of the enzyme is similar to subtilisin

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7 January 2021

Characterization of cDNA for murine tripeptidyl-peptidase II reveals alternative splicing

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7 January 2021

Subtilases: the superfamily of subtilisin-like serine proteases

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7 January 2021

Structure-function studies of recombinant murine tripeptidyl-peptidase II: the extra domain which is subject to alternative splicing is involved in complex formation

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7 January 2021

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Minimization of variation in the response to different proteins of the Coomassie blue G dye-binding assay for protein

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7 January 2021

Distribution of tripeptidyl-peptidase II in the central nervous system of rat

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7 January 2021

Dissecting the catalytic triad of a serine protease

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7 January 2021

Association and dissociation of the tripeptidyl-peptidase II complex as a way of regulating the enzyme activity

1 reference

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7 January 2021

The insert within the catalytic domain of tripeptidyl-peptidase II is important for the formation of the active complex

1 reference

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7 January 2021

Subtilisin--an enzyme designed to be engineered

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7 January 2021

10.1016/S1570-9639(02)00468-5

Identifiers

DOI

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1 December 2017

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