A novel enzymic activity of phenylalanyl transfer ribonucleic acid synthetase from baker's yeast: zinc ion induced transfer ribonucleic acid independent hydrolysis of adenosine triphosphate

Biochemistry ◽  
1980 ◽  
Vol 19 (8) ◽  
pp. 1676-1680 ◽  
Author(s):  
Gabor L. Igloi ◽  
Friedrich Von der Haar ◽  
Friedrich Cramer
Keyword(s):  
Adenosine Triphosphate ◽  
Ribonucleic Acid ◽  
Zinc Ion ◽  
Enzymic Activity ◽  
Baker’S Yeast ◽  
Baker's Yeast ◽  
Hydrolysis Of

scholarly journals The nucleotide sequence of cysteine transfer ribonucleic acid from baker's yeast. Products of complete digestion with pancreatic ribonuclease and ribonuclease T1

1976 ◽  
Vol 153 (2) ◽  
pp. 437-446 ◽  
Author(s):  
N J Holness ◽  
G Atfield
Keyword(s):  
Nucleotide Sequence ◽  
Ribonucleic Acid ◽  
Baker’S Yeast ◽  
Baker's Yeast ◽  
Brief Treatment ◽  
Ribonuclease T1 ◽  
Pancreatic Ribonuclease ◽  
Adenylic Acid ◽  
Complete Digestion ◽  
Conventional Methods

1. The nucleotide chain of tRNA Cys from baker's yeast was readily split at the anticolon into two large fragments by brief treatment with ribonuclease T1.2. The whole molecule and the two derived large fragments were completely digested with (a) pancreatic ribonuclease and (b) ribonuclease T1. The fragments present in each of the digests were separated and sequenced by conventional methods. 3. The groups of fragments derived from the two methods of digestion were entirely compatible with each other. 4. The molecule is 75 nucleotides long, but, as isolated, lacks the terminal adenosine and the neighboring cytidylic acid residue. The minor nucleotides 1-methyladenylic acid, 7-methylguanylic acid, 5-methylcytidylic acid and N6 (γγ-dimethylallyl)adenylic acid (isopentenyladenylic acid) were identified.

Isolation of Seryl and Phenylalanyl Ribonucleic Acid Synthetases from Baker's Yeast*

Biochemistry ◽  
1965 ◽  
Vol 4 (7) ◽  
pp. 1434-1442 ◽  
Author(s):  
Maynard H. Makman ◽  
Giulio L. Cantoni
Keyword(s):  
Ribonucleic Acid ◽  
Baker’S Yeast ◽  
Baker's Yeast

Purification and properties of three endopeptidases from baker's yeast

1989 ◽  
Vol 35 (2) ◽  
pp. 295-303 ◽  
Author(s):  
Jerzy Nowak ◽  
Hsin Tsai
Keyword(s):  
Ethyl Ester ◽  
Baker’S Yeast ◽  
Molecular Forms ◽  
Acid Proteinase ◽  
Baker's Yeast ◽  
Ph Optimum ◽  
Protein Substrates ◽  
Milk Clotting ◽  
Hydrolysis Of ◽  
Milk Clotting Activity

Three endopeptidases, proteinases A, B, and Y, were purified from baker's yeast, Saccharomyces cerevisiae. Two molecular forms of proteinase A (PRA), Mr 45 000 and 54 000, (estimated on SDS-PAGE) were obtained. Both forms were inhibited by pepstatin and other acid proteinase inhibitors. The enzyme digested hemoglobin most rapidly at pH 2.7–3.2 and casein at pH 2.4–2.8 and 5.5–6.0. The optimum pH for hydrolysis of protein substrates could be shifted to about 5 with 4–6 M urea. Urea also stimulated the enzyme activity by 30–50%. As other acid proteinases, the enzyme preferentially cleaved peptide bonds of X–Tyr and X–Phe type. A proteinase B (PRB) preparation of approximately Mr 33 000 possessed milk clotting activity and showed an inhibition pattern typical for seryl-sulfhydryl proteases. The purified enzyme could be stabilized with 40% glycerol and stored at −20 °C without significant loss of activity for several months. The third endopeptidase, designated PRY, of Mr 72 000 when estimated by Sephadex G-100 gel filtration, had properties resembling PRA and PRB. Similar to PRB, it could be inhibited by up to 90% with phenylmethylsulfonyl fluoride and para-chloromercuribenzoate and preferentially hydrolyzed the Leu15–Tyr16 peptide bond of the oxidized β-chain of insulin. On the other hand, contrary to PRB, it had neither milk clotting activity nor esterolytic activity toward N-acetyl-L-tyrosine ethyl ester and N-benzoyl-L-tyrosine ethyl ester and was stable during storage at −20 °C without glycerol. The enzyme also showed a lower pH optimum for hydrolysis of casein yellow than PRB. Similar to PRA, 4 M urea shifted its pH optimum for hydrolysis of protein substrates. PRY degraded apo-aminopeptidase Y much more efficiently than PRB or a PRA–PRB mixture. The possibility of PRY being a precursor form of PRA and PRB is discussed.Key words: yeast, endopeptidase, proteinase, purification.

scholarly journals The presence of dolichol in a lipid diphosphate N-acetylglucosamine from Saccharomyces cerevisiae (baker's yeast)

1978 ◽  
Vol 169 (3) ◽  
pp. 505-508 ◽  
Author(s):  
F Reuvers ◽  
P Boer ◽  
F W Hemming
Keyword(s):  
Saccharomyces Cerevisiae ◽  
High Pressure ◽  
Liquid Chromatography ◽  
High Pressure Liquid Chromatography ◽  
Alkaline Hydrolysis ◽  
Baker’S Yeast ◽  
Baker's Yeast ◽  
Isoprene Unit ◽  
Lipid Moiety ◽  
Hydrolysis Of

The lipid moiety of a lipid diphosphate N-acetylglucosamine, an intermediate in glycosylation of proteins, was studied. Ozonolysis of the compound gave evidence for an alpha-saturated isoprene unit. Alkaline hydrolysis of the glycolipid, followed by high-pressure liquid chromatography, showed the presence of a series of polyprenol homologues identical with those isolated directly from Saccharomyces cerevisiae (baker's yeast). No particular homologue was preferred in the enzymic transfer of N-acetylglucosamine 1-phosphate to endogenous dolichol monophosphate.

Fractionation of Peptides Obtained by Tryptic Hydrolysis of Baker's Yeast Cytochrome c

1964 ◽  
Vol 56 (3) ◽  
pp. 230-240 ◽  
Author(s):  
KOITI TITANI ◽  
MASAMI KIMURA ◽  
J. VANĚČEK ◽  
HIRONORI MURAKAMI ◽  
KOZO NARITA
Keyword(s):  
Cytochrome C ◽  
Baker’S Yeast ◽  
Baker's Yeast ◽  
Hydrolysis Of ◽  
Tryptic Hydrolysis

scholarly journals The nucleotide sequence of cysteine transfer ribonucleic acid from baker's yeast. Identification of the products from partial degradation of the molecule and derivation of the complete sequence

1976 ◽  
Vol 153 (2) ◽  
pp. 447-454 ◽  
Author(s):  
N J Holness ◽  
G Atfield
Keyword(s):  
Nucleotide Sequence ◽  
Ribonucleic Acid ◽  
Complete Sequence ◽  
Baker’S Yeast ◽  
Baker's Yeast ◽  
Brief Treatment ◽  
Yeast Identification ◽  
Pancreatic Ribonuclease ◽  
Correct Sequence ◽  
Partial Degradation

1. A series of large oligonucleotide fragments derived from tRNA Cys, were separated chromatographically and the sequence of each was deduced by examination of the products of digestion with pancreatic and T1 ribonucleases. 2. The location of the specific cleavage points in the nucleotide chain was similar to that produced by brief treatment with pancreatic ribonuclease. 3. The fragments could be arranged into two alternative sequences. The correct sequence was deduced by the sequential removal and identification of the first nine nucleotides from the 3′-end of the terminal half of the molecules.

scholarly journals CRYSTALLINE INORGANIC PYROPHOSPHATASE ISOLATED FROM BAKER'S YEAST

1952 ◽  
Vol 35 (3) ◽  
pp. 423-450 ◽  
Author(s):  
M. Kunitz
Keyword(s):  
Molecular Weight ◽  
Enzymatic Hydrolysis ◽  
Isoelectric Point ◽  
Calcium Ions ◽  
Baker’S Yeast ◽  
Thiamine Pyrophosphate ◽  
Inorganic Pyrophosphatase ◽  
Baker's Yeast ◽  
Inorganic Pyrophosphate ◽  
Hydrolysis Of

Crystalline inorganic pyrophosphatase has been isolated from baker's yeast. The crystalline enzyme is a protein of the albumin type with an isoelectric point near pH 4.8. Its molecular weight is of the order of 100,000. It contains about 5 per cent tyrosine and 3.5 per cent tryptophane. It is most stable at pH 6.8. The new crystalline protein acts as a specific catalyst for the hydrolysis of inorganic pyrophosphate into orthophosphate ions. It does not catalyze the hydrolysis of the pyrophosphate radical of such organic esters as adenosine di- and triphosphate, or thiamine pyrophosphate. Crystalline pyrophosphatase requires the presence of Mg, Co, or Mn ions as activators. These ions are antagonized by calcium ions. Mg is also antagonized by Co or Mn ions. The rate of the enzymatic hydrolysis of inorganic pyrophosphate is proportional to the concentration of enzyme and is a function of pH, temperature, concentration of substrate, and concentration of activating ion. The approximate conditions for optimum rate are: 40°C. and pH 7.0 at a concentration of 3 to 4 x 10–3 M Na4P2O7 and an equivalent concentration of magnesium salt. The enzymatic hydrolysis of Na4P2O7 or K4P2O7 proceeds to completion and is irreversible under the conditions at which hydrolysis is occurring. Details are given of the method of isolation of the crystalline enzyme.

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