Aminopeptidases in the Acidic Fraction of the Yeast Autolysate

Masuda, Tasaburo; Hata, Toshiyuki

doi:10.1080/00021369.1975.10861611

Cited by 4 publications

(6 citation statements)

References 1 publication

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“…The first step involves cleavage of the tripeptide to glycine and 0.74 Met-Gly, followed by hydrolysis of the dipeptide by the aminopeptidase itself. It is well known that yeast aminopeptidases are capable of cleaving dipeptides (5,15,17). The negative response DYE of the aminopeptidases here to the dipeptides MARKER tested may be due in part to the assay conditions ,attern for Leu-Leu-employed and the time required for the assay.…”

Section: Resultsmentioning

confidence: 96%

“…It has been demonstrated by several workers that various microorganisms, including yeasts, contain aminopeptidase, carboxypeptidase, and dipeptidase activities (11,15,20,23,25,26,28). Peptidases are capable of providing amino acids for cell growth by hydrolyzing peptides.…”

mentioning

confidence: 99%

“…More recently, Frey and Rohm (6) demonstrated the existence of three aminopeptidases and a single dipeptidase in partially fractionated cell extracts of S. cerevisiae. Several yeast peptidases have also been purified and characterized to varying degrees (3,5,9,15,17,24). However, we still do not know the total number and types of peptidases present in S. cerevisiae.…”

mentioning

confidence: 99%

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Peptidase activities in Saccharomyces cerevisiae

Rose¹,

Becker²,

Naider³

1979

J Bacteriol

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At least four distinct aminopeptidase activities and a single dipeptidase activity were found in cell extracts of a leucine-lysine auxotroph of Saccharomyces cerevisiae. The assay for peptidase activity involved polyacrylamide gel electrophoresis followed by an enzyme-coupled activity staining procedure. The aminopeptidases had largely overlapping specificities but could be distinguished from one another by their electrophoretic mobilities and activities toward different peptide substrates. Substrates tested included both free and blocked diand tripeptides and amino acid derivatives.

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Section: Resultsmentioning

confidence: 96%

mentioning

confidence: 99%

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confidence: 99%

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Peptidase activities in Saccharomyces cerevisiae

Rose¹,

Becker²,

Naider³

1979

J Bacteriol

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“…In addition to the vacuolar aminopeptidases yscI and yscCo and the periplasmic aminopeptidase ysclI a variety of soluble aminopeptidase activities have been found [105,107,109,126]. Enzyme activity named aminopeptidase ysclII of either 30 kDa [105] or 34 kDa [126] molecular weight has been described.…”

Section: Other Soluble Proteinasesmentioning

confidence: 99%

Proteinase function in yeast: Biochemical and genetic approaches to a central mechanism of post-translational control in the eukaryote cell

Rendueles

1988

FEMS Microbiology Letters

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“…One unit of aminopeptidase activity was defined as that which released 1 mol p-nitroanilide min-' . The molar absorption coefficient is 9900 1 mol-' cm-I at 405 nm (Masuda et al, 1975).…”

Section: Radiolabelling Of Gelatinmentioning

confidence: 99%

Age-dependent changes in extracellular proteins, aminopeptidase and proteinase activities in Frankia isolate BR

Muller

Benoist²,

Diem³

et al. 1991

Journal of General Microbiology

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To investigate protein secretion by the nitrogen-fixing actinomycete Frunkiu isolate BR, we designed a rapid DEAE adsorption, salt elution and Biogel P6DG desalination method to concentrate protein from the growth medium. Secreted proteins reached a maximum concentration (5.6 mg I-') in the medium at growth arrest. Analysis by SDS-PAGE detected up to 63 extracellular polypeptides when Frunkiu cells were grown under stirred conditions in BAP medium supplemented with phosphatidylcholine and MES buffer and 65 proteins in stirred BAP media alone. The pattern of extracellular polypeptides changed during growth. Several extracellular proteolytic activities were detected and compared with intracellular ones. The substrate specificity of the extracellular and intracellular aminopeptidase activities were the same. Also, the electrophoretic migration patterns of secreted and intracellular aminopeptidases could not be distinguished. Secretion of the proline-specific aminopeptidase FAP 3.BR appeared to be the only one that arrested at the end of the exponential phase of growth. At least 15 proteinases (PF) were secreted: 10 had the same electrophoretic mobility as their intracellular counterparts after SDS-gelatine-PAGE while five (PF-39.5, PF-38.5, PF-36.5, PF-25.5 and PF-20.5 kDa) had a different electrophoretic mobility and, therefore, appeared to be exclusively extracellular. At least seven extracellular proteinases appeared to increase coordinately in activity shortly before growth arrest.

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Aminopeptidases in the Acidic Fraction of the Yeast Autolysate

Cited by 4 publications

References 1 publication

Peptidase activities in Saccharomyces cerevisiae

Peptidase activities in Saccharomyces cerevisiae

Proteinase function in yeast: Biochemical and genetic approaches to a central mechanism of post-translational control in the eukaryote cell

Age-dependent changes in extracellular proteins, aminopeptidase and proteinase activities in Frankia isolate BR

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