(Q36781989)

English

Prolyl oligopeptidase catalysis. Reactions with thiono substrates reveal substrate-induced conformational change to be the rate-limiting step

scientific article published on May 1993

In more languages

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

16 August 2017

Prolyl oligopeptidase catalysis. Reactions with thiono substrates reveal substrate-induced conformational change to be the rate-limiting step (English)

1 reference

Europe PubMed Central

PubMed publication ID

16 August 2017

author name string

Polgár L

1

1 reference

Europe PubMed Central

PubMed publication ID

16 August 2017

Kollt E

2

1 reference

Europe PubMed Central

PubMed publication ID

16 August 2017

Hollósi M

3

1 reference

Europe PubMed Central

PubMed publication ID

16 August 2017

language of work or name

0 references

publication date

1 May 1993

1 reference

Europe PubMed Central

PubMed publication ID

16 August 2017

1 reference

Europe PubMed Central

PubMed publication ID

16 August 2017

322

1 reference

Europe PubMed Central

PubMed publication ID

16 August 2017

3

1 reference

Europe PubMed Central

PubMed publication ID

16 August 2017

227-230

1 reference

Europe PubMed Central

PubMed publication ID

16 August 2017

A new family of serine-type peptidases related to prolyl oligopeptidase

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2893%2981575-K

21 January 2018

Structural relationship between lipases and peptidases of the prolyl oligopeptidase family

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2893%2981575-K

21 January 2018

Transition-state stabilization at the oxyanion binding sites of serine and thiol proteinases: hydrolyses of thiono and oxygen esters

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2893%2981575-K

21 January 2018

Serine Proteases: Structure and Mechanism of Catalysis

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2893%2981575-K

21 January 2018

pH-dependent mechanism in the catalysis of prolyl endopeptidase from pig muscle

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2893%2981575-K

21 January 2018

Prolyl endopeptidase catalysis. A physical rather than a chemical step is rate-limiting

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2893%2981575-K

21 January 2018

Cleavage of the Lys196-Ser197 bond of prolyl oligopeptidase: enhanced catalytic activity for one of the two active enzyme forms

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2893%2981575-K

21 January 2018

MECHANISM OF ACTION OF PROTEOLYTIC ENZYMES.

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2893%2981575-K

21 January 2018

Thionation reactions of lawesson's reagents

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2893%2981575-K

21 January 2018

Oligopeptidases, and the emergence of the prolyl oligopeptidase family.

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2893%2981575-K

21 January 2018

Cysteine proteases: the S2P2 hydrogen bond is more important for catalysis than is the analogous S1P1 bond

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2893%2981575-K

21 January 2018

Buffers of constant ionic strength for studying pH-dependent processes

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2893%2981575-K

21 January 2018

Identifiers

10.1016/0014-5793(93)81575-K

1 reference

Europe PubMed Central

PubMed publication ID

16 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

16 August 2017

ResearchGate publication ID

0 references

Sitelinks

Wikipedia(0 entries)

Wikibooks(0 entries)

Wikinews(0 entries)

Wikiquote(0 entries)

Wikisource(0 entries)

Wikiversity(0 entries)

Wikivoyage(0 entries)

Wiktionary(0 entries)

Multilingual sites(0 entries)

Retrieved from "https://www.wikidata.org/w/index.php?title=Q36781989&oldid=1656144833"