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1 second substrate in a "ping-pong" mechanism accepting a proton.
2 f approximately 6.5-7 acts as a general base accepting a proton as the beta-hydroxy acid is oxidized
3 presented show that this quinonoid may also accept a proton at C(4)' of the cofactor to yield alpha-
4 us hydroxide ion results from its ability to accept a proton from a neighboring water molecule; yet,
5 that an aspartate acts as a general base to accept a proton from the 3-hydroxyl of Cm, concurrent wi
6 ion of the pyrimidine ring, and is poised to accept a proton from the C2 position of the thiazolium r
8 the key aspartate, Asp85, and its ability to accept a proton from the Schiff base during the photocyc
9 l His143 first serves as the general base to accept a proton from the zinc-bound water molecule in th
10 then protonated by the group that originally accepted a proton from the secondary amine of saccharopi
11 ys an essential role in catalysis, likely by accepting a proton from the active site serine, thus inc
13 lamine is then facilitated by the same group accepting a proton from the carbinolamine hydroxyl to ge
14 ropose that Glu-133 acts as a proton shuttle accepting a proton from the metal-bound water and subseq
15 late group of Asp256 enables the reaction by accepting a proton from the primer O3'group, thus activa
17 serves as a base to initiate the reaction by accepting a proton from the steroid and the nonionized h
18 lyase, where it may serve as a general base accepting a proton from the succinyl group during cataly
19 g water between Asp-145 and the 3'-phosphate accepts a proton from another water to stabilize the bri
22 s represents D294, and during catalysis D294 accepts a proton from K199 to allow K199 to act as a gen
23 nding and to act as an active-site base that accepts a proton from sLys to enable the subsequent amin
24 gest the requirement for a general base that accepts a proton from the 2-hydroxyl group of either sub
25 chanism is suggested in which a general base accepts a proton from the 2-hydroxyl of Fru 6-P concomit
26 s positioned to act as the general base that accepts a proton from the 2-hydroxyl of malate during th
27 The second group, which has a pK(a) of 5.6, accepts a proton from the alpha-amine of glutamate so th
29 l-serine are bound, an enzymic general base accepts a proton from the l-serine side chain hydroxyl a
30 a likely candidate for the general base that accepts a proton from the malate hydroxyl in the oxidati
32 nd, at the same time, the nitrogen lone pair accepts a proton from the other aspartate; and, bond bre
33 saccharopine bind, a group with a pKa of 6.2 accepts a proton from the secondary amine of saccharopin
34 e aforementioned selectivities by delivering/accepting a proton (H(+)) via its N-H bond cleavage/form
36 role of Arg(297) as a general base catalyst accepting a proton in the dehydrogenation of succinate.
37 n, the thermodynamically favored position to accept a proton on the flavin ring system is at N(5).
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