CAS 9046-67-7

Serine carboxypeptidase

Description:

Serine carboxypeptidase, with the CAS number 9046-67-7, is an enzyme that plays a crucial role in protein metabolism by catalyzing the hydrolysis of peptide bonds at the carboxyl-terminal end of proteins and peptides. This enzyme is classified as a serine protease due to the presence of a serine residue in its active site, which is essential for its catalytic activity. Serine carboxypeptidase is typically found in various biological systems, including the digestive systems of certain organisms, where it aids in the breakdown of dietary proteins into smaller peptides and amino acids. The enzyme exhibits specificity for certain amino acid residues at the C-terminus of substrates, influencing its activity and function. Additionally, it is often studied in the context of biochemical research and therapeutic applications, particularly in understanding protein processing and regulation. Its activity can be influenced by factors such as pH, temperature, and the presence of inhibitors or activators, making it a subject of interest in enzymology and biochemistry.

Formula: Unspecified

Synonyms:

• E.C. 3.4.12.1
• EC 3.4.12.1
• Carboxypeptidase, serine
• Carboxypeptidase C
• Serine carboxypeptidase

Carboxypeptidase C

CAS: 9046-67-7

Carboxypeptidase C removes COOH-terminal amino acids and others in peptides for biochemical studies.

Color and Shape: Solid

Ref: TM-T76168

Carboxypeptidase Y 01

CAS: 9046-67-7

A proteolytic enzyme which can cleave L-amino acids from the C-terminal of polypeptides

Ref: 3D-ECPY01.6

Carboxypeptidase Y, from S. cerevisiae, recombinant, lyophilized - ECPY001

CAS: 9046-67-7

Carboxypeptidase Y (EC 3.4.16.1) is an exopeptidase enzyme. It hydrolyzes peptide bonds of C-terminal residues and it remains active in the presence of urea at low to moderate concentrations. One unit of the Carboxypeptidase Y will hydrolyze 1.0 μmole of a chromogenic peptide substrate, releasing C-terminal alanine and generating a light-absorbing product. Carboxypeptidase Y has been obtained from yeast S. cerevisiae, has a broad substrate specificity and can therefore be used in sequence analysis of proteins. Carboxypeptidase Y has a temperature optimum in the 20 – 30 °C range and pH optimum between pH 6 and 7.

Ref: 3D-EC179334

Carboxypeptidase Y from baker's yeast

CAS: 9046-67-7

Carboxypeptidase Y (EC 3.4.16.1) is an exopeptidase enzyme. It hydrolyzes peptide bonds of C-terminal residues and it remains active in the presence of urea at low to moderate concentrations. One unit of the Carboxypeptidase Y will hydrolyze 1.0 μmole of a chromogenic peptide substrate, releasing C-terminal alanine and generating a light-absorbing product.

Purity: Min. 95%

Ref: 3D-FC49697