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Merck

77087

Sigma-Aldrich

ω-Transaminase, Aspergillus fumigatus

recombinant, expressed in E. coli, ≥0.20 U/mg

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About This Item

Número de CAS:
Comisión internacional de enzimas:
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in E. coli

form

powder

specific activity

≥0.20 U/mg

storage temp.

−20°C

Packaging

Bottomless glass bottle. Contents are inside inserted fused cone.

Unit Definition

1 U corresponds to the amount of enzyme which releases 1 μmol acetophenone per minute at 30°C. (R(−)-α-methyl-benzylamine as substrate).

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1 - Skin Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

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omega-Amino acid-pyruvate aminotransferase.
K Yonaha et al.
Methods in enzymology, 143, 500-504 (1987-01-01)
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
Beta alanine aminotransferase (s) from a plant source.
R A Stinson et al.
Biochemical and biophysical research communications, 34(1), 120-127 (1969-01-06)
T P West
Antonie van Leeuwenhoek, 77(1), 1-5 (2000-03-04)
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 was of interest to
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

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