Isolation And Characterization Of The Carboxypeptidase Y Inhibitor From Yeast

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A NOVEL GUANYL-PREFERABLE RIBONUCLEASE OF Bacillus polymyxa

by intracellular protein inhibitor of B. amyloliquefaciens RNase with the dissociation constant of 2.7x10 -12 M. Key words: ribonuclease, Bacillus polymyxa, isolation, substrate specificity, amino-acid sequence, specific protein-protein conlplex INTRODUCTION

RNA2: Clustering & motifs (Last week) - HUIT Sites Hosting

The specificity of carboxypeptidase Y may be altered by changing the hydrophobicity of the S'1 binding pocket. The structural basis for the altered substrate specificity of the R292D active site mutant of aspartate aminotransferase from E. coli. Thymidine kinase with altered substrate specificity of acyclovir resistant varicella-zoster virus.

JOURNAL OF BACTERIOLOGY Contents for Februairy

Isolation and Characterization of anEscherichia coli ruv Mutant Which Forms Non-septate Filaments After Low Doses of Ultraviolet Light Irradiation. NOZOMu OTSUJI, HIROAKI IYEHARA, ANDYOKoHIDESHIMA 337 Saturated Fatty Acid Mutant of Saccharomyces cerevisiae with an Intact Fatty Acid Synthetase. KARLH.

BIBLIOGRAPHY Abdelhak, S., Kalatzis, V., Heilig, R., Compain

180 Baticle, E. 1935. Le problème de la répartition. Comptes Rendus 201:862-864. Bier, M., and Nord, F. F. 1951. On the mechanism of enzyme action. XLVI. The effect of

The Squibb Institute for Medical Research (Received for

inhibitor, inhibited ACE competitively with a Ki of 1.5 /LM. Liver alcohol dehydrogenase and carboxypeptidase A, two other zinc-containing enzymes, were not inhibited at 150 /IM. In-hibition of ACE could not be reversed by divalent cations.

Current Research in Photosynthesis

The Characterization of a Potent, Naturally Occurring, ATPase Inhibitor (SIF) Isolated from the Halotolerant Algae Dunaliella 165 S. Selman-Reimer, B.R. Selm an Isolation, Purification and Characterization of Coupling Factor ATPase from Anacystis nidulans 169 H. Nemoto, Y. Ohta, T. Hisabori, K. Shinohara, H. Sakurai

Isolation, Characterization and Localization of the

The inhibitor is not affected by incubation with proteinase B but is inactivated by proteinase A and carboxypeptidase Y from yeast and by trypsin from bovine pancreas. The proteinase B inhibitor association constant was calculated to be 3.3 x lo9 M- and the enzyme inhibitor complex is stable at 25°C in the pH range 5-10.

Clustering by gene and/or condition Distance and similarity

The specificity of carboxypeptidase Y may be altered by changing the hydrophobicity of the S'1 binding pocket. The structural basis for the altered substrate specificity of the R292D active site mutant of aspartate aminotransferase from E. coli. Thymidine kinase with altered substrate specificity of acyclovir resistant varicella-zoster virus.

J. - Raines Lab

bovine pancreatic trypsin inhibitor carboxypeptidase Y Cys-Xaa-Cys Cys-Xaa-Xaa-Cys S, S' -dithiobis(2-nitrobenzoic acid) D,L-dithiothreitol ethylenediaminetetraacetic acid endoplasmic reticulum endoplasmic reticulum oxidoreductin 1 protein reduced glutathione oxidized glutathione high perfomance liquid chromatography insulin-like growth factor-I

Isolation and Characterization of the Carboxypeptidase Y

and carboxypeptidase Y. In the present paper we report the dissociation of intact carboxypeptidase Y inhibitor (IC) fronm the earlier described carboxypeptidase Y-IC complex (4, 5). The isolation and characterization of this inhibitor is also described. MATERIALS AND METHODS Carboxypeptidase A (treated with diisopropyl phospho-

Contents to volume 283 - CORE

Kuryatov. Y. Maulet. M.L. Malosio. V. Schmieden. H. Betz 73 The proteinase yscA-inhibitor, 1 , gene: Studies of cytoplasmic proteinase inhibitor deficiency on yeast physiology (FEBS 09693) P. Schu. D.H. Wolf 78 Structural features of stomach aldehyde dehydrogenase distin­ guish dimeric aldehyde dehydrogenase as a 'variable' en­

Microbial Cell Factories BioMed Central

A carboxypeptidase inhibitor from the tick Rhipicephalus bursa : isolation, cDNA cloning, recombinant ex pression, and characterization. J Biol Chem 2005, 280:3441-3448. 3. Peranen J, Rikkonen M, Hyvonen M, Kaariainen L: T7 vectors with modified T7lac promoter for expression of proteins in Escherichia coli Anal Biochem 1996, 236:371-373. 4.

Purification and Characterization of a Novel

activities in yeast that can catalyze the cleavage of the three COOH-terminal amino acids from the synthetic peptide substrate N-acetyl-KSKTK[S-farnesyl-Cys] VIM in vitro, a membrane-associated enzyme and two soluble activities, one of which has been identified as vacuolar carboxypeptidase Y (Hrycyna & Clarke, 1992).

Vam7p, a vacuolar SNAP-25 homolog, is required for SNARE

matured carboxypeptidase Y (Wada et al., 1992, 1997; Nichols et al., 1997). The phenotype of the Vam7p deletion 3270 mutant led us to ask whether it is a SNAP-25 homolog in the vacuolar SNARE complex. As shown in Figure 1B, Vam7p remains with the vacuoles during their isolation. Though Vam7p does not have a transmembrane domain,

Plant Physiology and Biochemistry

0.83, 1.0mM for native, bacterial and yeast protein, respectively. Both recombinant forms of IAInos synthase and the native enzyme also have the same optimal pH of 7.4 and all of them are inhibited by phe-nylmethylsulfonyl fluoride (PMSF), specific inhibitor of serine carboxypeptidases. 1. Introduction

Contents to volume 242 - CORE

Ohta. A. Matsui, Y. Nazawa, Y. Kagawa Cloning, sequencing and expression of the lipase gene from Pseudomonasfragi IFO-12049 in E. coli (FEB 06427) S. Aoyama, N. Yoshida. S. Inouye Characterization of a bovine acidic FGF cDNA clone and its expression in brain and retina (FEB 06453) J. Alterio, C. Halley, C. Brou.

Isolation of Yeast Mutants Defective in Protein Targeting to

yeast vacuole. The yeast vacuole seems analogous to the mammalian lysosome from the standpoint that a number of glycoprotein hydrolases are sequestered within the organelle (5). The intracellular passage of one such vacuolar enzyme, carboxypeptidase Y (CPY; EC 3.4.16.1), has been analyzed in yeast cells that exhibit temperature-conditional

THE OF BIOLOGICAL CHEMISTRY Vol. 255, No. 10, Issue 25, pp

4822 Yeast Proteinase A Inhibitor Regulatory Mutant icals were from Merck A. G. (Darrnstadt, Germany). Yeast Strains-The haploid yeast strains used in this work were strain S288C (e, mal -), obtained from R. K. Mortimer, and strain 4275-2A (a, mal-), our standard mating type a strain. B7 mutant was derived from S288C.

AUTHOR INDEX TO VOLUME 56 - COnnecting REpositories

Bai, Y. and R. Hayashi, A possible role for a single cysteine residue in carboxypeptidase Y Balestreri, E., M. Bracaloni, G. Montagnoli and R. A. Felicioli, Catalytically active azoaldolase: identification of cysteinyl residues involved in the diazothioether chromophores formation Barash, H., see S. Kahane

University of Groningen Engineering specificity and activity

inhibitor (1983) Biochemistry 22, 236-240 60. Jin, Y. and Kim, D.H. Inhibition stereochemistry of hydroxamate inhibitors for thermolysin (1998) Bioorg Med Chem Lett 8, 3518 61. Kester, W.R. and Matthews, B.W. Crystallographic study of the binding of dipeptide inhibitors to thermolysin: implications for the

Contents to volume 238 - CORE

Purification and characterization of two GTP-binding proteins of 22 kDa from human platelet membranes (FEB 06333) K. Nagafa, Y. Nozawa Purification and partial characterization of two &tins from the cactus Machaerocereus eruca (FEB 06344) E. Zenteno, H. Debray, J. Montreuil 5 9 13 17 22 27 31 35 39 43 49 56 61 67 71

Characterization, Recombinant Production and Structure

This unusually tight inhibitor is found in several isoforms in the snail and here we report the isolation and identification of four of them, the biochemical and cellular characterization of a main isoform and the development of an e cient recombinant production method in yeast. Also, the location of the inhibitor in the body of the snail

Isolation of defective in proteintargeting to the vacuole

Isolation ofyeast mutantsdefective in proteintargetingto the vacuole (carboxypeptidase Y/invertase/gene fusion/protein sorting) VYTASA. BANKAITIS, LIANNAM. JOHNSON, ANDSCOTTD. EMR Division ofBiology, California Institute ofTechnology, Pasadena, CA91125 Communicatedby GiuseppeAttardi, July 16, 1986 ABSTRACT We have constructed a PRCI-SUC2 gene

Studies on a Carboxypeptidase Y Mutant of Yeast and Evidence

In a previous paper we described the isolation and partial characterization of a mutant, which lacks the carboxypeptidase Y activity as judged by the absence of the esterolytic, amidase and proteolytic activity associated with carboxypeptidase Y [6 1. In the follow- ing work we tried to answer the following questions.

Glycoprotein biosynthesis in yeast

that can be propagated in both yeast and Escherichia coli has greatly contributed to the isolation and manipulation of yeast genes (8). When glycosylation mutants are available, genes can be cloned by complementation of these mutants with yeast genomic libraries (5, 8-11). Because few S. cerevisiae genes contain introns, genomic libraries are

Isolation and Characterization ofthe Carboxypeptidase Y Inhibitor

and carboxypeptidase Y. Inthe present paper wereport the dissociation of intact carboxypeptidase Yinhibitor (IC) from the earlier described carboxypeptidase y-Ic complex (4, 5). The isolation and characterization of this inhibitor is also described. MATERIALS AND METHODS Carboxypeptidase A (treated with diisopropyl phospho-

Secretion Granules of Transplantable Pancreatic

inhibitor, or both, until use. For electrophoresis, both freshly prepared or stored zymogen granule extracts were solubilized for 3min at 100°C (Laemmli, 1970); electrophoresis was carried out in SDS/polyacrylamide cylindrical or slab gels according to Laemmli (1970). The gels were fixed and stained as described previously (Reddy & Kumar, 1977).

Purification and Partial Characterization of Human and

terminal residues were made with a carboxypeptidase obtained from bakers yeast (carboxypeptidase Y) (22). Kinetic studies of amino acid release by 2% (w/w) carboxypeptidase Y were performed at 37 in 0.01 M sodium acetate, pH 5.5. Primary Sequence and Amino Acid Analyses-Samples con-

Proteases & Phosphatases - G-Biosciences

During isolation and characterization of the proteins, proteases are released following cell or tissue lysis and degrade protein samples, which can reduce the quality of the protein sample for further analysis. In order to prevent degradation of the proteins, protease inhibitor cocktail is added, which help preserve the nature of the protein.

THE SODIUM-HYDROGEN EXCHANGER NHX1 DRIVES LATE ENDOSOME

in Bakers yeast, whose cellular functions have been studied in more detail. 2. Nhx1 and endocytosis Like NHE6 and NHE9 in neurons, yeast Nhx1 predominantly resides on Late Endosomes (LE) where it imports Na+ or K+ into the lumen in exchange for export of H+ into the cytoplasm. This function counteracts VMA activity to fine tune lumenal pH

Proteases and the emerging role of protease inhibitors in

genes (15-17). The yeast KEX2 gene product is a membrane-bound Cat-dependent subtilisin-like serine protease that is required for in vivo processing of pro-a-mating factor at paired basic residues (35). Use of polymerase chain reaction (PCR) with primers directed toward yeast Kex2 active-site regions led to the isolation of cDNAs representing mam-