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

Julius, David; Brake, Anthony J.; Blair, Lindley C.; Kunisawa, Riyo; Thorner, Jeremy

doi:10.1016/0092-8674(84)90442-2

Cited by 693 publications

(405 citation statements)

References 27 publications

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“…We called the enzyme proteinase yscF [7]. Using the artificial substrate Boc-Gln-Arg-Arg-7-amido-4-methylcoumarin the same enzyme was identified [8]. Several facts are in excellent agreement with the notion that this enzyme is the initial a-factor precursor processing catalyst.…”

Section: Introductionsupporting

confidence: 62%

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Some characteristics of hormone (pheromone) processing enzymes in yeast

1987

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The KEX2 gene-encoded, membrane-bound Ca 2 ÷-dependent thiol endoproteinase, proteinase yscF, responsible for processing of the precursor protein of the sex pheromone or-factor of the yeast Saccharomyces cerevisiae was solubilized from the membraneous fraction and partially purified. Gel filtration revealed an apparent Mr of the native protein of around 150000. Ca 2 ÷ concentration for half-maximal activity was in the micromolar range and concentration of the substrate Cbz-Tyr-Lys-Arg-4-nitroanilide for half-maximal velocity was 0.05 mM. The enzyme is able to cleave basic amino acids from the carboxy-terminus of peptides and probably involved in final maturation of the ~t-factor peptides generated by proteinase yscF is membrane-associated, active at neutral pH and responds strongly to the serine proteinase inhibitor phenylmethylsulfonyl fluoride as well as to -SH group blocking agents.

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Section: Introductionsupporting

confidence: 62%

“…Several facts are in excellent agreement with the notion that this enzyme is the initial a-factor precursor processing catalyst. (i) The enzyme is missing in a sterile mutant (kex2) which accumulates inactive orfactor precursor [7,8].…”

Section: Introductionmentioning

confidence: 99%

Some characteristics of hormone (pheromone) processing enzymes in yeast

1987

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“…These preprosequences are processed twice. The presequence is cleaved by the ERleader peptidase, whereas the second one is cleaved in the late Golgi by a functional equivalent of S. cerevisiae Kex2 [40,41]. Two basic residues (KR or RR) precede the second cleavage site.…”

Section: Secretionmentioning

confidence: 99%

The methylotrophic yeast Hansenula polymorpha: a versatile cell factory

Dijk

Faber

Kiel

et al. 2000

Enzyme and Microbial Technology

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“…Previous work has indicated that in a family of similar peptide substrates, the same peptide bond is cleaved by a given endoprotease; i.e. either in between the dibasic pair for the pro-enkephalin , on the COOH-terminal side of the doublet in the case of pro-alpha-mating factor [6], pro-ocytocin/neurophysin (pro-OT/Np) [7,8] processing enzyme, or else the NHz-terminal side of the Arg-Lys doublet in the case of somatostatin-28 [9]. Preliminary examination of the observations made in various laboratories, suggested that the peptide substrate conformation may play an important role in the specification of the cleavage loci [11,12] and that the interactions between the lateral domains of the constituting amino acids of a substrate and the appropriate subsites of the peptidase mainly govern the selection of the peptide bond involved in the hydrolytic process.…”

Section: Introductionmentioning

confidence: 99%

Role of peptide substrate structure in the selective processing of peptide prohormones at basic amino acid pairs by endoproteases

et al. 1988

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Three putative processing enzymes, each with defined action in a prohormone system, a ‘pro‐ocytocin‐neurophysin convertase’ from bovine neurohypophysis secretory granules, a ‘Leu‐enkephalin Arg6 generating enzyme’ from human CSF and the endoprotease from the ‘S‐28 convertase’ complex of rat brain cortex, were tested for their ability to hydrolyze peptides deriving from pro‐ocytocin, pro‐enkephalin B and pro‐somatostatin, respectively at pairs of basic amino acids. The observations suggest that structural parameters specified by the peptide region around the dibasic moieties govern recognition by the enzyme and define which peptide bond is hydrolyzed.

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

Cited by 693 publications

References 27 publications

Some characteristics of hormone (pheromone) processing enzymes in yeast

Some characteristics of hormone (pheromone) processing enzymes in yeast

The methylotrophic yeast Hansenula polymorpha: a versatile cell factory

Role of peptide substrate structure in the selective processing of peptide prohormones at basic amino acid pairs by endoproteases

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