Activities and cellular localization of yeast proteases and their inhibitors

Lenney, James F.; Matile, Philippe; Wiemken, A.; Schellenberg, Maya; Meyer, J.

doi:10.1016/0006-291x(74)90350-7

Cited by 133 publications

(50 citation statements)

References 9 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Human cathepsin D is localized in lysosomes (reviewed by Hasilik, [20]) and yeast proteinase A is localized in vacuoles (vacuoles in yeast are equivalent to lysosomes) [21] and both are major intracellular aspartic proteinases, while cathepsin E is localized intracellularly but extra-lysosomally [22]. Human cathepsin D is targeted to lysosomes by the mannose-6-phosphate (M6P) targeting pathway using the M6P marker and also by an alternative targeting pathway (reviewed by Kornfeld and Mellman, [23]).…”

Section: Sorting Of Aspartic Proteinasesmentioning

confidence: 99%

Multiple functions of pro‐parts of aspartic proteinase zymogens

et al. 1994

View full text Add to dashboard Cite

The importance of aspartic proteinases in human pathophysiology continues to initiate extensive research. With burgeoning information on their biological functions and structures, the traditional view of the role of activation peptides of aspartic proteinases solely as inhibitors of the active site is changing. These peptide segments, or pro-parts, am deemed important for correct folding, targeting, and control of the activation of aspartic proteinase zymogens. Consequently, the primary structures of pro-parts reflect these functions. We discuss guidelines for formation of hypotheses derived from comparing the physiological function of aspartic proteinases and sequences of their pro-parts.

show abstract

Section: Sorting Of Aspartic Proteinasesmentioning

confidence: 99%

Multiple functions of pro‐parts of aspartic proteinase zymogens

et al. 1994

View full text Add to dashboard Cite

show abstract

“…baker's yeast, and Rhodotorula glutinis have both been shown to contain an intracellular n.d. = not determined serine carboxypeptidase (68,78) while extracellular counterparts have not been identified for either organism. Carboxypeptidase Y from baker's yeast resides primarily in the vacuoles like proteases A and B and aminopeptidase I (116). Specific inhibitors of each of these enzymes are located in the cytoplasm surrounding the vacuoles (16,39,118,119,125,146,161) presumably regulating proteolysis (39).…”

Section: Serine Carboxypeptidases From Fungimentioning

confidence: 99%

Serine carboxypeptidases. A review

Breddam

1986

Carlsberg Res. Commun.

180

130

View full text Add to dashboard Cite

Carboxypeptidases are proteolytic enzymes which only cleave the C-terminal peptide bond in polypeptides. Those characterized until now can, dependent on their catalytic mechanism, be classified as either metallo carboxypeptidases or as serine carboxypeptidases. Enzymes from the latter group are found in the vacuoles of higher plants and fungi and in the lysosomes of animal cells. Many fungi, in addition, excrete serine carboxypeptidases. Apparently, bacteria do not employ this group of enzymes.Most serine carboxypeptidases presumably participate in the intracellular turnover of proteins and some of them, in addition, release amino acids from extracellular proteins and peptides. However, prolyl carboxypeptidase which cleaves the C-terminal peptide bond of angiotensin II and III is a serine carboxypeptidase with a more specific function.Serine carboxypeptidases are usually glycoproteins with subunit molecular weights of 40,000 -75,000. Those isolated from fungi apparently contain only a single peptide chain while those isolated from higher plants and animals in most cases contain two peptide chains linked by disulfide bridges. However, a number of the enzymes aggregate forming dimers and oligomers.It is probable that the well-known catalytic mechanism of the serine endopeptidases is also employed by the serine carboxypeptidases but presumably with the difference that the plQ of the catalytically essential histidyl residue is somewhat lower in the carboxypeptidases than in the endopeptidases. However, the leaving group specificity of these two groups of enzymes differ since the carboxypeptidases only release C-terminal amino acids from peptides (peptidase activity) and not longer peptide fragments. In addition, they release C-terminal amino acid amides (peptidyl amino acid amide hydrolase activity) or ammonia (amidase activity) from peptide amides and alcohols from peptide esters (esterase activity) and this property they share with the serine endopeptidases. Like other proteolytic enzymes the serine carboxypeptidases contain binding sites which secure the interaction between enzyme and substrate. In this laboratory, the properties of these have been studied for three serine carboxypeptidases, i.e. carboxypeptidase Y from yeast and malt carboxypeptidases I and II, by means of kinetic studies, chemical modifications of amino acid side-chains located at these binding sites and exchange of such amino acid residues by site-directed mutagenesis.Serine carboxypeptidases, such as carboxypeptidase Y and malt carboxypeptidase II which are available in large quantities, can be applied for several purposes. Their broad specificity and ability to release amino acids from the C-terminus of a peptide chain can be employed in determination of amino acid sequences, and their ability to catalyze transpeptidation reactions and aminolysis ofpeptide esters can be employed to exchange C-terminal amino acid residues in peptides and in step-wise synthesis ofpolypeptides, respectively. The type of reactions catalyzed by these enzymes is l...

show abstract

“…Mutant ascospores contained the activity of the two other known vacuolar proteinases, proteinase B and carboxypeptidase Y. An inhibitory protein of proteinase A which is located in the cytoplasm combines with the vacuolar proteinase A upon cell breakage [4]. In cell extracts this inhibitor can be inactivated by proteinase B [15].…”

Section: Proteinuse a Mutantsmentioning

confidence: 99%

“…Until the recent detection of a variety of new proteolytic enzymes [2] besides the three aminopeptidases, one dipeptidase and two carboxypeptidases, only two endoproteinases (proteinase A and proteinase B) had been found in S. cerevisiae [3] (for review see [I]). Both proteinases are localized in the vacuole of the yeast cell [4]. From studies m vitro proteinase A and proteinase B have been proposed to play a central role, either singly or together, in inactivation in vivo of a variety of enzymes active in the pathway of gluconeogenesis [5,6] and in activation in vivo of a vital enzyme for growth, namely chitin synthetase .…”

mentioning

confidence: 99%

Analysis of Proteinase A Function in Yeast

Mechler

Wolf

1981

European Journal of Biochemistry

View full text Add to dashboard Cite

Yeast mutants lacking proteinase A were isolated. One of these mutants (Hb I) is characterized in detail. The mutation called pral segregates 2: 2 in meiotic tetrads indicating a single gene mutation. N o anti-(proteinase A) cross-reacting material can be detected. Diploids heterozygous for praI show gene dosage. Thus, it appears that PRAl might be the structural gene for proteinase A.Results obtained with this mutant show that proteinase A is not a vital component of the vegetative cell cycle. The mutant exhibits normal mitotic growth under rich and poor growth conditions and shows normal mating. Enzymes subject to carbon catabolite inactivation and inactivation of NADP-dependent glutamate dehydrogenase, processes which were proposed to be of proteolytic nature, are not affected by the absence of proteinase A. However, protein degradation under sporulation conditions is about 30 ; ( reduced in proteinasc A mutant cells. The differentiation process of spordation is also disturbed leading to a 40 reduced sporulation frequency in mutant cells.

show abstract

Activities and cellular localization of yeast proteases and their inhibitors

Cited by 133 publications

References 9 publications

Multiple functions of pro‐parts of aspartic proteinase zymogens

Multiple functions of pro‐parts of aspartic proteinase zymogens

Serine carboxypeptidases. A review

Analysis of Proteinase A Function in Yeast

Contact Info

Product

Resources

About