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1 ype pumps evolved from enzymes that catalyze phosphoryl group transfer.
2 es of known tertiary structure that catalyze phosphoryl group transfer.
3 -determining step for this poor substrate is phosphoryl group transfer.
4 that offsets the kinetic isotope effect for phosphoryl group transfer.
5 ng that substrate processing occurs via slow phosphoryl group transfer (12 +/- 4 s(-1)) followed by t
6 e and that kcat is partially limited by both phosphoryl group transfer (40-100 s-1) and product relea
7 d to product by a kinetic mechanism in which phosphoryl group transfer (45 s-1) and product release (
8 es lie exclusively in the rate constants for phosphoryl group transfer and not in substrate absorptio
9 tein conformational change that occurs after phosphoryl group transfer and prior to product release.
10 t with a "virtual" transition state in which phosphoryl group transfer and product release steps part
13 ADP so that both the binding of ligands and phosphoryl group transfer at the active site can be moni
15 bly the opening of the activation loop after phosphoryl group transfer but preceding product release.
16 trates is critical to the catalysis of (thio)phosphoryl group transfer, but there has been no systema
18 e protein intermediate which is required for phosphoryl group transfer from the sensor kinase SLN1 to
19 nformations, each with His455 positioned for phosphoryl group transfer from/to one of the substrates.
20 sult suggests a novel two-base mechanism for phosphoryl group transfer in a phosphorylated sugar.
23 2+ site of P-type pumps and the mechanism of phosphoryl group transfer is proposed and tested by demo
25 (k(cat)) is rate-limited by both reversible phosphoryl group transfer (k(forward) approximately 0.2
26 lation, the calcium pump appears to catalyze phosphoryl group transfer less efficiently than the sodi
27 nzyme of known structure that also catalyzes phosphoryl group transfer make a direct role for the pos
29 y, catalyzes the Mg(2+)-dependent reversible phosphoryl group transfer of the N-phosphoryl group of p
30 nthase activity is an indication of the high phosphoryl group transfer potential of bis-PP-IP4 and ma
31 tabilize ATP and myelin basic protein in the phosphoryl group transfer reaction, accounting for the e
34 ent is due to an increase in the rate of the phosphoryl group transfer step by approximately 60,000-f
36 or peptide I are linear, indicating that the phosphoryl group transfer step is associated with a sing
37 rom a 3,000-fold increase in the rate of the phosphoryl group transfer step with a more moderate incr
40 n human alpha(1) Na,K-ATPase participates in phosphoryl group transfer, the charge was progressively
41 fer protein or kinase (X) is responsible for phosphoryl group transfer to CtrA in the proposed DivJ -
42 IKKbeta is required for IKKbeta activation, phosphoryl group transfer to IKKgamma, and acquisition o