Substrate Specificities and Kinetic Properties of Proteinase A from the Yeast Saccharomyces cerevisiae and the Development of a Novel Substrate

1998 ◽  
Vol 124 (1) ◽  
pp. 141-147 ◽  
Author(s):  
H. Kondo ◽  
Y. Shibano ◽  
T. Amachi ◽  
N. Cronin ◽  
K. Oda ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Kinetic Properties ◽  
Yeast Saccharomyces Cerevisiae ◽  
Substrate Specificities ◽  
Proteinase A

scholarly journals The selectivity of action of the aspartic-proteinase inhibitor IA3 from yeast (Saccharomyces cerevisiae)

1985 ◽  
Vol 231 (3) ◽  
pp. 777-779 ◽  
Author(s):  
T Dreyer ◽  
M J Valler ◽  
J Kay ◽  
P Charlton ◽  
B M Dunn
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Proteinase Inhibitor ◽  
Aspartic Proteinase ◽  
Significant Extent ◽  
Aspartic Proteinases ◽  
Yeast Saccharomyces Cerevisiae ◽  
Naturally Occurring ◽  
Proteinase A

The ability of the aspartic-proteinase inhibitor IA3 from yeast (Saccharomyces cerevisiae) to affect the activities of a range of mammalian and microbial aspartic proteinases was examined. The inhibitor appeared to be completely selective in that only the aspartic proteinase A from yeast was inhibited to any significant extent. IA3 thus represents the first example of a totally specific, naturally occurring, aspartic-proteinase inhibitor.

scholarly journals The mechanism for the ATP-induced uncoupling of respiration in mitochondria of the yeast Saccharomyces cerevisiae

1995 ◽  
Vol 307 (3) ◽  
pp. 657-661 ◽  
Author(s):  
S Prieto ◽  
F Bouillaud ◽  
E Rial
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Membrane Potential ◽  
Cytochrome C ◽  
Oxidative Phosphorylation ◽  
Cytochrome C Oxidase ◽  
Kinetic Properties ◽  
Yeast Saccharomyces Cerevisiae ◽  
Saccharomyces Cerevisiae Mitochondria ◽  
Low Efficiency ◽  
Respiratory Chain Activity

We have recently reported that ATP induces an uncoupling pathway in Saccharomyces cerevisiae mitochondria [Prieto, Bouillaud, Ricquier and Rial (1992) Eur. J. Biochem. 208, 487-491]. The presence of this pathway would explain the reported low efficiency of oxidative phosphorylation in S. cerevisiae, and may represent one of the postulated energy-dissipating mechanisms present in these yeasts. In this paper we demonstrate that ATP exerts its action in two steps: first, at low ATP/Pi ratios, it increases the respiratory-chain activity, probably by altering the kinetic properties of cytochrome c oxidase. Second, at higher ATP/Pi ratios, an increase in membrane permeability leads to a collapse in membrane potential. The ATP effect on cytochrome c oxidase corroborates a recent report showing that ATP interacts specifically with yeast cytochrome oxidase, stimulating its activity [Taanman and Capaldi (1993) J. Biol. Chem. 268, 18754-18761].

scholarly journals Comparison of the effects of Ca2+, adenine nucleotides and pH on the kinetic properties of mitochondrial NAD+-isocitrate dehydrogenase and oxoglutarate dehydrogenase from the yeast Saccharomyces cerevisiae and rat heart

1994 ◽  
Vol 303 (2) ◽  
pp. 461-465 ◽  
Author(s):  
B J Nichols ◽  
M Rigoulet ◽  
R M Denton
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Isocitrate Dehydrogenase ◽  
Rat Heart ◽  
Adenine Nucleotides ◽  
Amino Acid Sequences ◽  
Kinetic Properties ◽  
Yeast Saccharomyces Cerevisiae ◽  
Rat Heart Mitochondria ◽  
Oxoglutarate Dehydrogenase ◽  
Regulatory Properties

The regulatory properties of NAD(+)-isocitrate dehydrogenase and oxoglutarate dehydrogenase in extracts of yeast and rat heart mitochondria were studied under identical conditions. Yeast NAD(+)-isocitrate dehydrogenase exhibits a low K0.5 for isocitrate and is activated by AMP and ADP, but is insensitive to ATP and Ca2+. In contrast, the rat heart NAD(+)-isocitrate dehydrogenase was insensitive to AMP, but was activated by ADP and by Ca2+ in the presence of ADP or ATP. Both yeast and rat heart oxoglutarate dehydrogenase were stimulated by ADP, but only the heart enzyme was activated by Ca2+. All the enzymes studied were activated by decreases in pH, but to differing extents. The effects of Ca2+, adenine nucleotides and pH were through K0.5 for isocitrate or 2-oxoglutarate. These observations are discussed with reference to the deduced amino acid sequences of the constituent subunits of the enzymes, where they are available.

scholarly journals Functional Analysis of Two l-Arabinose Transporters from Filamentous Fungi Reveals Promising Characteristics for Improved Pentose Utilization in Saccharomyces cerevisiae

2015 ◽  
Vol 81 (12) ◽  
pp. 4062-4070 ◽  
Author(s):  
Jingen Li ◽  
Jing Xu ◽  
Pengli Cai ◽  
Bang Wang ◽  
Yanhe Ma ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Sugar Transport ◽  
Biomass Accumulation ◽  
Kinetic Properties ◽  
High Identity ◽  
Content Type ◽  
Substrate Specificities ◽  
Dry Cell Weight ◽  
Dry Cell

ABSTRACTLimited uptake is one of the bottlenecks forl-arabinose fermentation from lignocellulosic hydrolysates in engineeredSaccharomyces cerevisiae. This study characterized two novell-arabinose transporters, LAT-1 fromNeurospora crassaand MtLAT-1 fromMyceliophthora thermophila. Although the two proteins share high identity (about 83%), they display different substrate specificities. Sugar transport assays using theS. cerevisiaestrain EBY.VW4000 indicated that LAT-1 accepts a broad substrate spectrum. In contrast, MtLAT-1 appeared much more specific forl-arabinose. Determination of the kinetic properties of both transporters revealed that theKmvalues of LAT-1 and MtLAT-1 forl-arabinose were 58.12 ± 4.06 mM and 29.39 ± 3.60 mM, respectively, with correspondingVmaxvalues of 116.7 ± 3.0 mmol/h/g dry cell weight (DCW) and 10.29 ± 0.35 mmol/h/g DCW, respectively. In addition, both transporters were found to use a proton-coupled symport mechanism and showed only partial inhibition byd-glucose duringl-arabinose uptake. Moreover, LAT-1 and MtLAT-1 were expressed in theS. cerevisiaestrain BSW2AP containing anl-arabinose metabolic pathway. Both recombinant strains exhibited much fasterl-arabinose utilization, greater biomass accumulation, and higher ethanol production than the control strain. In conclusion, because of higher maximum velocities and reduced inhibition byd-glucose, the genes for the two characterized transporters are promising targets for improvedl-arabinose utilization and fermentation inS. cerevisiae.

scholarly journals Comparison of glyoxalase I purified from yeast (Saccharomyces cerevisiae) with the enzyme from mammalian sources

1979 ◽  
Vol 183 (1) ◽  
pp. 23-30 ◽  
Author(s):  
Ewa Marmstål ◽  
Anne-Charlotte Aronsson ◽  
Bengt Mannervik
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Rhodospirillum Rubrum ◽  
Glyoxalase I ◽  
Kinetic Properties ◽  
Yeast Saccharomyces Cerevisiae ◽  
Physiological Concentration ◽  
Physiological Importance ◽  
Evolutionary Origins ◽  
Diffusion Controlled ◽  
Km Value

Glyoxalase I from yeast (Saccharomyces cerevisiae) purified by affinity chromatography on S-hexylglutathione–Sepharose 6B was characterized and compared with the enzyme from rat liver, pig erythrocytes and human erythrocytes. The molecular weight of glyoxalase I from yeast was, like the enzyme from Rhodospirillum rubrum and Escherichia coli, significantly less (approx. 32000) than that of the enzyme from mammals (approx. 46000). The yeast enzyme is a monomer, whereas the mammalian enzymes are composed of two very similar or identical subunits. The enzymes contain 1Zn atom per subunit. The isoelectric points (at 4°C) for the yeast and mammalian enzymes are at pH7.0 and 4.8 respectively; tryptic-peptide ‘maps’ display corresponding dissimilarities in structure. These and some additional data indicate that the microbial and the mammalian enzymes may have separate evolutionary origins. The similarities demonstrated in mechanistic and kinetic properties, on the other hand, indicate convergent evolution. The kcat. and Km values for the yeast enzyme were both higher than those for the enzyme from the mammalian sources with the hemimercaptal adduct of methylglyoxal or phenylglyoxal as the varied substrate and free glutathione at a constant and physiological concentration (2mm). Glyoxalase I from all sources investigated had a kcat./Km value near 107s−1·m−1, which is close to the theoretical diffusion-controlled rate of enzyme–substrate association. The initial-velocity data show non-Michaelian rate saturation and apparent non-linear inhibition by free glutathione for both yeast and mammalian enzyme. This rate behaviour may have physiological importance, since it counteracts the effects of fluctuations in total glutathione concentrations on the glyoxalase I-dependent metabolism of 2-oxoaldehydes.

PREPARASI DEINOCOCCUS RADIODURANS DAN KHAMIR DALAM MATERIAL KECAP L-DRYING SEBAGAI BAHAN UJI PROFISIENSI

2016 ◽  
Vol 13 (1) ◽  
pp. 93
Author(s):  
Titin Yulinery ◽  
Ratih M.Dewi
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Deinococcus Radiodurans ◽  
Test Preparation ◽  
Quality Parameters ◽  
Soy Sauce ◽  
Yeast Saccharomyces Cerevisiae ◽  
Microbiological Test ◽  
Bacterial Contaminants ◽  
Minimum Number ◽  
Important Quality

Tes kemampuan adalah salah satu kegiatan penting dalam pengendalian mutu dan jaminan kualitas mikrobiologi laboratorium untuk mengukur kompetensi analis dan analisis uji profisiensi membutuhkan persiapan Model mikroorganisme adalah kualitas standar dan validitas. Mikrobiologi uji kualitas produk kedelai utama diarahkan pada kehadiran Saccharomyces cerevisiae ragi (S. cerevisiae), S. Bailli, S. rouxii dankontaminan bakteri seperti Bacillus dan Deinococcus. Jenis ragi dan bakteri yang terlibat dalam proses dan dapat menjadi salah satu parameter kualitas penting dalam persiapan yang dihasilkan. Jumlah dan viabilitas bakteri dan ragi menjadi parameter utama dalam proses persiapan bahan uji. Jumlah tersebut adalah jumlah minimum yang berlaku dapat dianalisis. Jumlah ini harus dibawah 10 CFU diperlukan untuk menunjukkan tingkat hygienitas proses dan tingkat minimal kontaminasi. Viabilitas bakteri dan bahan tes ragi persiapan untuk tes kemahiran kecap yang diawetkan dengan L-pengeringan adalah teknik Deinococcus radiodurans (D. radiodurans) 16 tahun, 58 tahun S. cerevisiae, dan S. roxii 13 tahun. kata kunci: Viabilitas, Deinococcus, khamir, L-pengeringan, Proficiency AbstractProficiency test is one of the important activities in quality control and quality assurance microbiology laboratory for measuring the competence of analysts and analysis Proficiency test requires a model microorganism preparations are standardized quality and validity. Microbiological test of the quality of the main soy products aimed at thepresence of yeast Saccharomyces cerevisiae (S. cerevisiae), S. bailli, S. rouxii and bacterial contaminants such as Bacillus and Deinococcus. Types of yeasts and bacteria involved in the process and can be one of the important quality parameters in the preparation produced. The number and viability of bacteria and yeasts become themain parameters in the process of test preparation materials. The amount in question is the minimum number that is valid can be analyzed. This amount must be below 10 CFU required to indicate the level of hygienitas process and the minimum level of contamination. Viability of bacteria and yeast test preparation materials for proficiencytest of soy sauce that preserved by L-drying technique is Deinococcus radiodurans ( D. radiodurans ) 16 years, 58 years S. cerevisiae, and S. roxii 13 years. key words : Viability, Deinococcus, Khamir, L-drying, Proficiency

Sign in / Sign up

Export Citation Format

Share Document