ChemicalBook--->CAS DataBase List--->9046-67-7

9046-67-7

9046-67-7 Structure

9046-67-7 Structure
IdentificationBack Directory
[Name]

CARBOXYPEPTIDASE W
[CAS]

9046-67-7
[Synonyms]

EC 3.4.16.1
EC 3.4.16.6
IUB: 3.4.16.5
E.C. 3.4.16.5
E.C. 3.4.12.1
Yeast proteinase C
CARBOXYPEPTIDASE W
CARBOXYPEPTIDASE Y
Yeast proproteinase C
SERINE CARBOXYPEPTIDASE
Carboxypeptidase, serine
CARBOXYPEPTIDASE Y, YEAST
Lysosomal carboxypeptidase A
CARBOXYPEPTIDASE W USP/EP/BP
CARBOXYPEPTIDASE W FROM WHEAT
Carboxypeptidase Y (from Yeast)
Carboxypeptidase Y,from Wheat
Native Wheat Carboxypeptidase W
PEPTIDYL-L-AMINO ACID HYDROXYLASE
CARBOXYPEPTIDASE Y FROM BAKERS YEAST
CARBOXYPEPTIDASE Y FROM YEAST SEQUENCING
CARBOXYPEPTIDASE Y FROM BAKER'S YEAST, ~ 20 U/MG
CARBOXYPEPTIDASE Y FROM BAKER'S YEAST, >60 U/MG*
carboxypeptidase y from baker's yeast (s. cerevisiae)
CARBOXYPEPTID. Y F. BAKER'S YEAST,LYOPH. , STAB, ~12 U/MG
Carboxypeptidase Y from baker''s yeast from baker''s yeast
Peptidyl-L-amino acid Hydrolase, Serine Carboxypeptidase
CPase Y Y, Serine-type carboxypeptidase, Peptidyl-L-amino-acid hydolase
Carboxypeptidase Y from baker's yeast (S. cerevisiae) lyophilized powder, >=50 units/mg protein
[EINECS(EC#)]

232-934-1
[MDL Number]

MFCD00130723
Chemical PropertiesBack Directory
[storage temp. ]

−20°C
[form ]

powder
[color ]

white
[Water Solubility ]

Soluble in water.
[Specific Activity]

≥50units/mg protein
Safety DataBack Directory
[Symbol(GHS) ]

Exclamation Mark (GHS07)Health Hazard (GHS08)
GHS07,GHS08
[Signal word ]

Danger
[Hazard statements ]

H315-H319-H334-H335
[Precautionary statements ]

P302+P352-P305+P351+P338
[Hazard Codes ]

Xn
[Risk Statements ]

36/37/38-42
[Safety Statements ]

22-24-26-36/37-45
[WGK Germany ]

1
[F ]

10-21
Hazard InformationBack Directory
[Uses]

Carboxypeptidase Y from yeast is used for C-terminal sequencing of proteins. Also for C-terminal modification of proteins and peptides. Due to its amidase action, it is applied to the sequence analysis of peptides having amidated COOH-terminal groups such as oxytocin and vasopressin.
[Biological Activity]

The glycoprotein has a molecular weight of about 61,000has a nitrogen content of 12.74%. It is a single polypeptide chain of 442 residues with 16 residues of glucosamine in the carbohydrate moiety. Lysine is at the NH2 terminus and -Asp-Ser-Thr-Leu is the COOH-terminal sequence. The principal action of the enzyme is to remove COOH-terminal residues from polypeptide chains. It is used as a vacuolar marker enzyme for studies on protein transport and localization.
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