40972
ω-Transaminase, Aspergillus terreus
recombinant, expressed in E. coli, ≥0.10 U/mg
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About This Item
Numéro CAS:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54
Produits recommandés
Produit recombinant
expressed in E. coli
Niveau de qualité
Forme
powder
Activité spécifique
≥0.10 U/mg
Température de stockage
−20°C
Conditionnement
Bottomless glass bottle. Contents are inside inserted fused cone.
Définition de l'unité
1 U corresponds to the amount of enzyme which releases 1 μmol acetophenone per minute at 30°C. (R(−)-α-methyl-benzylamine as substrate).
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
Classification des risques
Resp. Sens. 1 - Skin Sens. 1
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
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Enzymatic studies on the metabolism of beta-alanine.
O HAYAISHI et al.
The Journal of biological chemistry, 236, 781-790 (1961-03-01)
J S Shin et al.
Bioscience, biotechnology, and biochemistry, 65(8), 1782-1788 (2001-10-02)
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 JS2F, Bacillus thuringiensis JS64, and Vibrio fluvialis JS17 showed good
K Yonaha et al.
The Journal of biological chemistry, 267(18), 12506-12510 (1992-06-25)
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 were purified and sequenced by Edman degradation.
Hyungdon Yun et al.
Applied and environmental microbiology, 70(4), 2529-2534 (2004-04-07)
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 (aptA) was cloned. The gene was functionally expressed in
J-S Shin et al.
Applied microbiology and biotechnology, 61(5-6), 463-471 (2003-04-11)
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 chromatography and a subunit
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