Structural and enzymatic characterization of a purified prohormone-processing enzyme: secreted, soluble Kex2 protease (Q24563308)

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English	Structural and enzymatic characterization of a purified prohormone-processing enzyme: secreted, soluble Kex2 protease	scientific article

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instance of

scholarly article

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title

Structural and enzymatic characterization of a purified prohormone-processing enzyme: secreted, soluble Kex2 protease (English)

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author

Charles Brenner

object named as

C Brenner

series ordinal

1

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author name string

R S Fuller

series ordinal

2

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language of work or name

English

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publication date

1 February 1992

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published in

Proceedings of the National Academy of Sciences of the United States of America

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volume

89

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issue

3

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page(s)

922-6

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cites work

Structural homology between the human fur gene product and the subtilisin-like protease encoded by yeast KEX2

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Human fur gene encodes a yeast KEX2-like endoprotease that cleaves pro-beta-NGF in vivo

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24 March 2017

Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-alpha-factor

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24 March 2017

Yeast α factor is processed from a larger precursor polypeptide: The essential role of a membrane-bound dipeptidyl aminopeptidase

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24 March 2017

Structure, biosynthesis, and localization of dipeptidyl aminopeptidase B, an integral membrane glycoprotein of the yeast vacuole

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24 March 2017

Yeast prohormone processing enzyme (KEX2 gene product) is a Ca2+-dependent serine protease

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PubMed Central

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24 March 2017

Localization of components involved in protein transport and processing through the yeast Golgi apparatus

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PubMed Central

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24 March 2017

Hormone processing and membrane-bound proteinases in yeast

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PubMed Central

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24 March 2017

Yeast KEX2 genes encodes an endopeptidase homologous to subtilisin-like serine proteases

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PubMed Central

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24 March 2017

Characterization of KEX2-encoded endopeptidase from yeast Saccharomyces cerevisiae

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PubMed Central

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24 March 2017

Serine Proteases: Structure and Mechanism of Catalysis

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24 March 2017

Secretion and autoproteolytic maturation of subtilisin

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27 September 2017

Enzymes required for yeast prohormone processing

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PubMed Central

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27 September 2017

A view of acidic intracellular compartments

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PubMed Central

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27 September 2017

Secretion of heterologous proteins directed by the yeast alpha-factor leader.

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PubMed Central

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27 September 2017

Processing of precursors by dipeptidylaminopeptidases: a case of molecular ticketing

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PubMed Central

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27 September 2017

cDNA sequence of two distinct pituitary proteins homologous to Kex2 and furin gene products: tissue-specific mRNAs encoding candidates for pro-hormone processing proteinases

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PubMed Central

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27 September 2017

Three proteolytic systems in the yeast saccharomyces cerevisiae.

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27 September 2017

Cloning and primary sequence of a mouse candidate prohormone convertase PC1 homologous to PC2, Furin, and Kex2: distinct chromosomal localization and messenger RNA distribution in brain and pituitary compared to PC2.

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PubMed Central

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27 September 2017

Immunolocalization of Kex2 protease identifies a putative late Golgi compartment in the yeast Saccharomyces cerevisiae

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PubMed Central

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27 September 2017

Identification of a cDNA encoding a second putative prohormone convertase related to PC2 in AtT20 cells and islets of Langerhans

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PubMed Central

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27 September 2017

Posttranslational processing of the prohormone-cleaving Kex2 protease in the Saccharomyces cerevisiae secretory pathway

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PubMed Central

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27 September 2017

Proteolytic conversion of proinsulin into insulin. Identification of a Ca2+-dependent acidic endopeptidase in isolated insulin-secretory granules

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PubMed Central

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30 May 2018

Calcium-dependent KEX2-like protease found in hepatic secretory vesicles converts proalbumin to albumin.

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PubMed Central

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30 May 2018

Intracellular targeting and structural conservation of a prohormone-processing endoprotease

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PubMed Central

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30 May 2018

Identification of a human insulinoma cDNA encoding a novel mammalian protein structurally related to the yeast dibasic processing protease Kex2.

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PubMed Central

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30 May 2018

Structural and functional integrity of specificity and catalytic sites of trypsin.

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PubMed Central

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19 June 2018

Sequence of the preprotoxin dsRNA gene of type I killer yeast: multiple processing events produce a two-component toxin

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PubMed Central

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28 November 2018

Three-dimensional structure of proteinase K at 0.15-nm resolution

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https://pubmed.ncbi.nlm.nih.gov/1736307

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Rational modification of enzyme catalysis by engineering surface charge

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/1736307

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12 December 2020

based on heuristic

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The action of factor Xa on peptide p-nitroanilide substrates: substrate selectivity and examination of hydrolysis with different reaction conditions

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/1736307

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Site-directed mutagenesis as a probe of enzyme structure and catalysis: tyrosyl-tRNA synthetase cysteine-35 to glycine-35 mutation

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/1736307

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

DOI

10.1073/PNAS.89.3.922

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ADS bibcode

1992PNAS...89..922B

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PMC publication ID

48357

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PubMed publication ID

1736307

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ResearchGate publication ID

21420095

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