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3 ed conformations of the beta-subunit for the alpha-aminoacrylate and quinonoid forms of the enzyme.
4 en the alpha-site and the external aldimine, alpha-aminoacrylate, and quinonoid forms of the beta-sit
5 le is positioned with C3 in contact with the alpha-aminoacrylate C(beta) and aligned for nucleophilic
6 bstrate L-Ser, destabilizes the enzyme-bound alpha-aminoacrylate, E(A-A), and quinonoid species, E(Q)
7 allosteric site in the internal aldimine and alpha-aminoacrylate external aldimine forms of OASS; (iv
8 etic isotope effects of approximately 2-3 on alpha-aminoacrylate formation when the alpha-(2)H-labele
9 s via a ping-pong kinetic mechanism in which alpha-aminoacrylate in Schiff base with the active site
11 irst half-reaction, conversion of OAS to the alpha-aminoacrylate intermediate and acetate, is rate-li
12 bond-forming reaction between the CysM-bound alpha-aminoacrylate intermediate and the thiocarboxylate
13 onversion of the internal Schiff base to the alpha-aminoacrylate intermediate at any concentration of
15 ff base preferentially partitions toward the alpha-aminoacrylate intermediate compared to OAS being r
17 ticity 50% that of wild-type enzyme, and the alpha-aminoacrylate intermediate has a molar ellipticity
18 rates and inhibitors; however, the predicted alpha-aminoacrylate intermediate has not been previously
19 the external aldimine but does not form the alpha-aminoacrylate intermediate on addition of OAS, sug
20 dimine followed by the slow formation of the alpha-aminoacrylate intermediate on addition of OAS.
21 e first-order rate constant for decay of the alpha-aminoacrylate intermediate to give pyruvate and am
22 order rate constant for disappearance of the alpha-aminoacrylate intermediate was measured over the p
24 enzyme tryptophan synthase, reactions of the alpha-aminoacrylate intermediate with the nucleophiles i
25 used to characterize the tryptophan synthase alpha-aminoacrylate intermediate, a defining species for
26 the sulfhydrylase reaction, formation of the alpha-aminoacrylate intermediate, limits the overall rea
27 stals does not result in the formation of an alpha-aminoacrylate intermediate, suggesting that the cr
32 he first direct spectroscopic observation of alpha-aminoacrylate intermediates in the reactions of TP
33 ypyridine, a subsequent slow reaction of the alpha-aminoacrylate is observed, which may be due to imi
34 w absorption band at 338 nm, assigned to the alpha-aminoacrylate, is observed with these substrates.
35 that soybean (Glycine max) CAS and OASS form alpha-aminoacrylate reaction intermediates from Cys and
36 The >25-fold activation of the alpha-site by alpha-aminoacrylate Schiff base formation at the beta-si
38 al 5'-phosphate at the beta-site to give the alpha-aminoacrylate Schiff base intermediate, E(A-A), is
39 e of the L-Ser Schiff base, E(Aex1), and the alpha-aminoacrylate Schiff base intermediate, E(A-A); in
40 the quinonoid state to give indoline and the alpha-aminoacrylate Schiff base, E(A-A), both in the abs
41 tophan (DIT), reacts with the beta-site, the alpha-aminoacrylate Schiff base, E(A-A), is formed and t
42 ction at the beta-subunit to form either the alpha-aminoacrylate Schiff base, E(A-A), or quinonoid sp
44 of phenol then has been proposed to give an alpha-aminoacrylate Schiff base, which releases iminopyr
45 nd, and NH(4)(+)-bound enzymes stabilize the alpha-aminoacrylate species, E(A-A), while Na(+) binding