Amine Transaminase

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The substrate specificity, enantioselectivity and structure of the (R)-selective amine : pyruvate transaminase from Nectria haematococca

UNLABELLED During the last decade the use of transaminases for the production of pharmaceutical and fine chemical intermediates has attracted a great deal of attention. Transaminases are versatile biocatalysts for the efficient production of amine intermediates and many have (S)-enantiospecificity. Transaminases with (R)-specificity are needed to expand the applications of these enzymes in bioc...

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Alteration of the Donor/Acceptor Spectrum of the (S)-Amine Transaminase from Vibrio fluvialis

To alter the amine donor/acceptor spectrum of an (S)-selective amine transaminase (ATA), a library based on the Vibrio fluvialis ATA targeting four residues close to the active site (L56, W57, R415 and L417) was created. A 3DM-derived alignment comprising fold class I pyridoxal-5'-phosphate (PLP)-dependent enzymes allowed identification of positions, which were assumed to determine substrate sp...

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Crystallization and preliminary X-ray diffraction studies of the (R)-selective amine transaminase from Aspergillus fumigatus.

The (R)-selective amine transaminase from Aspergillus fumigatus was expressed in Escherichia coli and purified to homogeneity. Bright yellow crystals appeared while storing the concentrated solution in the refrigerator and belonged to space group C222(1). X-ray diffraction data were collected to 1.27 Å resolution, as well as an anomalous data set to 1.84 Å resolution that was suitable for S-SAD...

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One-pot biocatalytic amine transaminase/acyl transferase cascade for aqueous formation of amides from aldehydes or ketones†‡

Biocatalytic acylation/amidation is well-known and has been applied for decades but it has often been limited to the use of organic solvents to avoid hydrolysis. The acyl transferase from Mycobacterium smegmatis (MsAcT) is an enzyme that can perform trans-acylations in aqueous solution. Only a few hydrolases can catalyze trans-acylation in water and MsAcT also has the ability to act as a perhyd...

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Glutamic Aspartic Transaminase

Aspartate and glutamate react instantaneously with the pyridoxal form of the pig heart glutamic aspartic transaminase (1) to yield the corresponding keto acid, converting the enzymebound pyridoxal phosphate to bound pyridoxamine phosphate (2). Other amino acids such as methionine sulfoxide, methionine sulfone, and alanine react much more slowly with the enzyme, but the reaction itself appears t...

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ژورنال

عنوان ژورنال: Agricultural and Biological Chemistry

سال: 1964

ISSN: 0002-1369

DOI: 10.1080/00021369.1964.10858262