Esterolytic Activity of Acid Carboxypeptidase fromAspergillus saitoi
نویسندگان
چکیده
منابع مشابه
Cloning and expression of the carboxypeptidase gene from Aspergillus saitoi and determination of the catalytic residues by site-directed mutagenesis.
Carboxypeptidase from Aspergillus saitoi removes acidic, neutral and basic amino acids as well as proline from the C-terminal position at pH 2-5. cpdS, a cDNA encoding A. saitoi carboxypeptidase, was cloned and expressed. Analysis of the 1816-nucleotide sequence revealed a single open reading frame coding for 523 amino acids. When A. saitoi carboxypeptidase cDNA was expressed in yeast cells, ca...
متن کاملCarboxypeptidase activity in human mycoplasmas.
Mycoplasma salivarium produced citrulline, ammonia, and ATP from N-benzoylglycyl-L-arginine. The activity was inhibited by EDTA and was therefore concluded to be due to an arginine-specific carboxypeptidase. The activity was also found to exist in M. orale, M. buccale, M. faucium, and M. hominis.
متن کاملParthenolide inhibits tubulin carboxypeptidase activity.
Microtubules are centrally involved in cell division, being the principal components of mitotic spindle. Tubulin, the constituent of microtubules, can be cyclically modified on its alpha-subunit by enzymatic removal of the COOH-terminal tyrosine residue by an ill-defined tubulin carboxypeptidase (TCP) and its readdition by tubulin tyrosine ligase (TTL). We and others have previously shown that ...
متن کاملThe catalytic activity of carboxypeptidase-degraded aldolase.
One approach to the general problem of the structure and function of enzymes involves proteolytic hydrolysis with examination of the structure, composition, and catalytic activity of the hydrolysis products. Fragments retaining partial enzyme activity have been obtained from trypsin and pepsin by autolysis (2, 3) and from trypsinogen by peptic digestion (4). Over half of the amino acid residues...
متن کاملThe specific esterase activity of carboxypeptidase.
It was recently found that the proteolytic enzymes trypsin (19 and chymotrypsin (2) possess specific esterase activity. In addition to catalyzing the hydrolysis of specific peptides (3-7), these enzymes also catalyze the hydrolysis of those esters which possess the structural environment of the specific peptides. In order to substantiate further the suggestion of Schwert et al. (1) that the spe...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1973
ISSN: 0002-1369
DOI: 10.1080/00021369.1973.10860734