1955
DOI: 10.1002/9780470122617.ch4
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Transamination

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Cited by 27 publications
(12 citation statements)
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“…TH is the enzyme responsible for catalyzing the conversion of the amino acid L-tyrosine to L-3,4-dihydroxyphenylalanine, 18,19 which is a precursor of the important neurotransmitters norepinephrine (noradrenaline) and epinephrine (adrenaline), and it catalyzes the rate-limiting step in the synthesis of catecholamines.…”
Section: Resultsmentioning
confidence: 99%
“…TH is the enzyme responsible for catalyzing the conversion of the amino acid L-tyrosine to L-3,4-dihydroxyphenylalanine, 18,19 which is a precursor of the important neurotransmitters norepinephrine (noradrenaline) and epinephrine (adrenaline), and it catalyzes the rate-limiting step in the synthesis of catecholamines.…”
Section: Resultsmentioning
confidence: 99%
“…Only significantly elevated AST was detected compared to control; therefore, we did not consider higher disruption of amino acid metabolism. Higher level of ATS would indicate a greater energy demand which is normally associated with synthesizing activities of the cell (Meister 1955). Slight increases in Ca 2+ level after exposure in MS 222 were reported by Congleton (2006) and Soivio et al (1977), but not significantly different from the control group.…”
Section: Discussionmentioning
confidence: 83%
“…This was supported by studies investigating the conversion of glutamate to other amino acids in pigeon muscles, started in 1936 by the Russian enzymologist Alexander E. Braunstein, which demonstrated that these reactions were catalyzed by pyridoxine-dependent enzymes (Braunstein and Kritzman, 1946). The ensuing discovery of the variety of reactions catalyzed by PLP-dependent enzymes, including transamination (Cammarata and Cohen, 1950;Meister, 1955;Jenkins and Sizer, 1957), racemization (Wood and Gunsalus, 1951), decarboxylation (Mandeles et al, 1954;Rothberg and Steinberg, 1957) and side-chain 5 elimination or rearrangement (Yanofsky and Reissig, 1953;Matsuo, 1958), was the starting point for research investigating the catalytic versatility of PLP and the mechanism whereby the protein component of the enzyme regulates cofactor chemistry (Snell, 1953;Ikawa and Snell, 1954;Longenecker, 1957a;Longenecker et al, 1957b) .…”
Section: Pyridoxal 5'-phosphate (Plp) Cofactormentioning
confidence: 94%