ω-Transaminase(S-amine) (Crude Enzyme)

Modify Date: 2024-01-05 07:16:29

ω-Transaminase(S-amine) (Crude Enzyme) Structure
ω-Transaminase(S-amine) (Crude Enzyme) structure
Common Name ω-Transaminase(S-amine) (Crude Enzyme)
CAS Number 9030-47-1 Molecular Weight N/A
Density N/A Boiling Point N/A
Molecular Formula N/A Melting Point N/A
MSDS Chinese USA Flash Point N/A
Symbol GHS08
GHS08
Signal Word Danger

 Use of ω-Transaminase(S-amine) (Crude Enzyme)


This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Reaction: L-alanine + 3-oxopropanoate = pyruvate + β-alanine

 Names

Name ω-Transaminase(S-amine) (Crude Enzyme)
Synonym More Synonyms

 ω-Transaminase(S-amine) (Crude Enzyme) Biological Activity

Description This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Reaction: L-alanine + 3-oxopropanoate = pyruvate + β-alanine

 Chemical & Physical Properties

No Any Chemical & Physical Properties

 Safety Information

Symbol GHS08
GHS08
Signal Word Danger
Hazard Statements H317-H334
Precautionary Statements P261-P280-P342 + P311
RIDADR NONH for all modes of transport

 Articles12

More Articles
The primary structure of omega-amino acid:pyruvate aminotransferase.

J. Biol. Chem. 267(18) , 12506-10, (1992)

The complete amino acid sequence of bacterial omega-amino acid:pyruvate aminotransferase (omega-APT) was determined from its primary structure. The enzyme protein was fragmented by CNBr cleavage, tryp...

Crystal structure analysis of omega-amino acid:pyruvate aminotransferase with a newly developed Weissenberg camera and an imaging plate using synchrotron radiation.

J. Biochem. 105(1) , 1-3, (1989)

The three-dimensional structure of omega-amino acid:pyruvate aminotransferase from Pseudomonas sp. F-126, an isologous alpha 4 tetramer containing pyridoxal 5'-phosphate (PLP) as a cofactor, has been ...

Lack of stringent stereospecificity in the inactivation of pyridoxal phosphate-dependent enzymes by suicide-substrates.

Prog. Clin. Biol. Res. 144A , 377-85, (1984)

 Synonyms

EC 2.6.1.18
β-alanine-pyruvate aminotransferase
β-alanine-α-alanine transaminase