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Isothiocyanyl Alanine as a Synthetic Intermediate for the Synthesis of Thioureayl Alanines and Subsequent Aminotetrazolyl Alanines

The Journal of Organic Chemistry, 2017
The synthesis of unnatural amino acids with small side-chain functionalities usable for further transformations is highly demanding for the expansion of the genetic code and other possible biotechnological applications. To this end, we wanted to report the utility of an unexplored unnatural amino acid, isothiocyanyl alanine (NCSAla = Ita), for the ...
Subhendu Sekhar Bag, Suranjan De
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Combinatorial alanine-scanning

Current Opinion in Chemical Biology, 2001
Combinatorial libraries of alanine-substituted proteins can be used to rapidly identify residues important for protein function, stability and shape. Each alanine substitution examines the contribution of an individual amino acid sidechain to the functionality of the protein.
Gregory A Weiss, G A Weiss
exaly   +3 more sources

Poem: A is for alanine

Biochemistry and Molecular Biology Education, 2005
AbstractThe poem below presents a brief review of amino acid abbreviations and structures. Among the featured facts are the following: histidine has a pKa close to the normal pH of the cytosol and therefore is an effective intracellular buffer, the R group of isoleucine is hydrophobic, and many protein kinases add a phosphate at the ‐OH site of ...
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Alanine dehydrogenases in mycobacteria

Journal of Microbiology, 2019
Since NAD(H)-dependent L-alanine dehydrogenase (EC 1.1.4.1; Ald) was identified as one of the major antigens present in culture filtrates of Mycobacterium tuberculosis, many studies on the enzyme have been conducted. Ald catalyzes the reversible conversion of pyruvate to alanine with concomitant oxidation of NADH to NAD+ and has a homohexameric ...
Ji-A, Jeong, Jeong-Il, Oh
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Regulation of gluconeogenesis by alanine

Biochimica et Biophysica Acta (BBA) - General Subjects, 1974
Abstract 1. 1. L -alanine and α-amino-isobutyric acid (0.5–10 mM) have been shown to stimulate glucose formation by isolated kidney tubules from fed and starved rats, with the substrates pyruvate, lactate, fructose, malate, fumarate, α-oxoglutarate and glycerol.
D, Friedrichs, W, Schoner
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DL-Alanine

Acta Crystallographica Section C Crystal Structure Communications, 2001
A determination of the structure of the title compound, C3H7NO2, leads to an accurate description of its molecular dimensions and crystal packing. As in the structure of the L-isomer, the molecules aggregate into alternating layers, each consisting of only one type of isomer. The molecules in each layer are interconnected through head-to-tail sequences
M, Subha Nandhini   +2 more
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Amperometric Alanine Electrode

Analytical Letters, 1993
Abstract An amperometric enzyme electrode for L-Alanine determination was developed. The probe is based on a platinum electrode which senses the hydrogen peroxide produced by the enzymatic reactions catalyzed by two enzymes: alanine aminotransferase (ALT) and glutamate oxidase.
PALLESCHI, GIUSEPPE   +5 more
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Brivanib alaninate for cancer

Expert Opinion on Investigational Drugs, 2011
Angiogenesis inhibition represents a rational therapeutic strategy in the management of solid tumors. Brivanib is a dual tyrosine kinase inhibitor with selectivity against VEFGR-2 and FGFR.This review provides an updated summary of preclinical and clinical experience with brivanib in cancer.
Ivan, Diaz-Padilla, Lillian L, Siu
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Serum alanine assay with an enzymic micromethod (L-alanine dehydrogenase)

Clinica Chimica Acta, 1978
L-Alanine was measured by an enzymic micromethod in serum after treatment with perchloric acid, as well as after ultrafiltration through collodium membrane filters. Serum L-alanine was also determined by an automated column chromatographic technique. Using the enzymic method, spuriously increased L-alanine levels could be obtained due to the absorbent ...
A, Berg, W, Gerok, J, Keul
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Inactivation of alanine aminotransferase by the neurotoxin β-cyano-L-alanine

Biochemical and Biophysical Research Communications, 1980
Abstract β-Cyano-L-alanine inactivates pig heart alanine aminotransferase. The nitrile and enzyme form a freely dissociable Michaelis complex which rearranges to a form of inactive enzyme. The inactivated enzyme slowly recovers activity at 25° in 100 mM phosphate buffer, pH 7.4. The observations are consistent with a mechanism of inactivation similar
T A, Alston   +3 more
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