Results 361 to 370 of about 251,409 (391)

Continuous flow synthesis of chiral amines in organic solvents: immobilization of E. coli cells containing both ω-transaminase and PLP.

Organic Letters, 2014
E. coli cells containing overexpressed (R)-selective ω-transaminase and the cofactor PLP were immobilized on methacrylate beads suitable for continuous flow applications.
L. Andrade, W. Kroutil, T. Jamison
semanticscholar   +1 more source

Serum transaminases in kwashiorkor

The Journal of Pediatrics, 1962
Determinations of serum glutamic oxaloacetic and glutamic pyruvic transaminases in children with kwashiorkor failed to show differences between children with “serious” or “early” disease; there was also no change in the concentration of the enzymes after 3 weeks of treatment.
openaire   +3 more sources

ω-Transaminase-catalyzed asymmetric synthesis of unnatural amino acids using isopropylamine as an amino donor.

Organic and biomolecular chemistry, 2013
Isopropylamine is an ideal amino donor for reductive amination of carbonyl compounds by ω-transaminase (ω-TA) owing to its cheapness and high volatility of a ketone product.
Eul‐Soo Park, Joo‐Young Dong, J. Shin   +2 more
semanticscholar   +1 more source

Infra-nuclear Distribution of Transaminases

Nature, 1964
IT has previously been shown1 that isolated calf thymus nuclei prepared by the sucrose-CaCl2 procedure2 contain a free amino-acid pool. Of the free amino-acids, glutamic acid represents about 40 per cent. The presence of such a relatively large amount of glutamic acid suggests its rapid synthesis, or its formation by metabolic conversion from other ...
Tung-Yue Wang, Kuang Mei Wang
openaire   +3 more sources

Use of ω-Transaminase Enzyme Chemistry in the Synthesis of a JAK2 Kinase Inhibitor

, 2013
ω-Transaminase enzyme chemistry provides an excellent methodology to build synthetically useful chiral amines from their corresponding ketones. An application of this methodology, providing a long-term commercial manufacturing route to a JAK2 kinase ...
Lianne Frodsham, M. Golden, S. Hard, Martin N. Kenworthy, David J. Klauber, K. Leslie, C. S. MacLeod, Rebecca E. Meadows, K. Mulholland, J. Reilly, C. Squire, Simone Tomasi, D.A.L. Watt, A. Wells   +13 more
semanticscholar   +1 more source

[15] Glutamate-ornithine transaminases

1985
Publisher Summary This chapter provides an overview of glutamate–ornithine transaminases. The simplest assay of δ-ornithine transaminase is based on the formation of a dihydroquinazolinium between Δ 1 -pyrroline-5-carboxylate and o-aminobenzaldehyde. Several radiochemical assays are discussed in the chapter.
openaire   +3 more sources

Aminotransferase (Transaminase) Isoenzymes

1970
Of the numerous enzymes which reversibly catalyse the transfer of an amino group from an amino acid to an α-keto acid, the two which have been most extensively studied are aspartate aminotransferase (formerly known as glutamate-oxaloacetate transaminase) and alanine aminotransferase (formerly known as glutamate-pyruvate transaminase).
openaire   +2 more sources

MITOCHONDRIAL ASPARTATE TRANSAMINASE

The Lancet, 1970
A.M. Nanji, T.R.C. Boyde, S.N. Farmer
openaire   +3 more sources

[11] Glutamate-aspartate transaminase

1985
Publisher Summary This chapter focuses on glutamate–aspartate transaminase, an enzyme that is present in microorganisms, plants, and in all animal and human tissues. Its ubiquity attests to its metabolic importance. In addition, in higher organisms, the enzyme exists in soluble (sGOT) and mitochondrial (mGOT) forms.
openaire   +3 more sources

Determination of transaminase.

Methods of biochemical analysis, 2000
Alton Meister, Anita J. Aspen
openaire   +3 more sources