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

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

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, trypsin, and Staphylococcus aureus V8 digestions. The peptides ...

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 determined at 2.0 A resolution. The diffraction data were c...

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

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

Omega-amino acid: pyruvate aminotransferase: subunit structure, spectrometric properties and amino acid sequence around pyridoxyl lysine.

Prog. Clin. Biol. Res. 144B , 329-38, (1984)

One-pot synthesis of amino-alcohols using a de-novo transketolase and beta-alanine: pyruvate transaminase pathway in Escherichia coli.

Biotechnol. Bioeng. 96(3) , 559-69, (2007)

Biocatalysis continues to emerge as a powerful technique for the efficient synthesis of optically pure pharmaceuticals that are difficult to access via conventional chemistry. The power of biocatalysis can be enhanced if two or more reactions can be achieved ...

omega-Amino acid:pyruvate transaminase from Alcaligenes denitrificans Y2k-2: a new catalyst for kinetic resolution of beta-amino acids and amines.

Appl. Environ. Microbiol. 70(4) , 2529-34, (2004)

Alcaligenes denitrificans Y2k-2 was obtained by selective enrichment followed by screening from soil samples, which showed omega-amino acid:pyruvate transaminase activity, to kinetically resolve aliphatic beta-amino acid, and the corresponding structural gene...

Purification, characterization, and molecular cloning of a novel amine:pyruvate transaminase from Vibrio fluvialis JS17.

Appl. Microbiol. Biotechnol. 61(5-6) , 463-71, (2003)

A transaminase from Vibrio fluvialis JS17 showing activity toward chiral amines was purified to homogeneity and its enzymatic properties were characterized. The transaminase showed an apparent molecular mass of 100 kDa as determined by gel filtration chromato...

Comparison of the omega-transaminases from different microorganisms and application to production of chiral amines.

Biosci. Biotechnol. Biochem. 65(8) , 1782-8, (2001)

Microorganisms that are capable of (S)-enantioselective transamination of chiral amines were isolated from soil samples by selective enrichment using (S)-alpha-methyl-benzylamine ((S)-alpha-MBA) as a sole nitrogen source. Among them, Klebsiella pneumoniae JS2...

Properties of the bound coenzyme and subunit structure of omega-amino acid:pyruvate aminotransferase.

J. Biol. Chem. 258(4) , 2260-5, (1983)

Role of cytosine deaminase and beta-alanine-pyruvate transaminase in pyrimidine base catabolism by Burkholderia cepacia.

Antonie van Leeuwenhoek 77(1) , 1-5, (2000)

A determination of the possible role of the salvage enzyme cytosine deaminase or beta-alanine-pyruvate transaminase in the catabolism of the pyrimidine bases uracil and thymine by the opportunistic pathogen Burkholderia cepacia ATCC 25416 was undertaken. It w...