Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:4.1.2.42 (DTA)
 1,693 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Glutamic acid-148, an active-site residue of diphtheria toxin identified by photoaffinity labeling with NAD, was replaced with aspartic acid, glutamine, or serine by directed mutagenesis of the F2 fragment of the toxin gene. Wild-type and mutant F2 proteins were synthesized in Escherichia coli, and the corresponding enzymic fragment A moieties (DTA) were derived, purified, and characterized. The Glu----Asp (E148D), Glu----Gln (E148Q), and Glu----Ser (E148S) mutations caused reductions in NAD:EF-2 ADP-ribosyltransferase activity of ca. 100-, 250-, and 300-fold, respectively, while causing only minimal changes in substrate affinity. The effects of the mutations on NAD-glycohydrolase activity were considerably different; only a 10-fold reduction in activity was observed for E148S, and the E148D and E148Q mutants actually exhibited a small but reproducible increase in NAD-glycohydrolytic activity. Photolabeling by nicotinamide-radiolabeled NAD was diminished ca. 8-fold in the E148D mutant and was undetectable in the other mutants. The results confirm that Glu-148 plays a crucial role in the ADP-ribosylation of EF-2 and imply an important function for the side-chain carboxyl group in catalysis. The carboxyl group is also important for photochemical labeling by NAD but not for NAD-glycohydrolase activity. The pH dependence of the catalytic parameters for the ADP-ribosyltransferase reaction revealed a group in DTA-wt that titrates with an apparent pKa of 6.2-6.3 and is in the protonated state in the rate-determining step.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Active-site mutations of diphtheria toxin: effects of replacing glutamic acid-148 with aspartic acid, glutamine, or serine. 198 Feb 8

The paper describes a study on the fluorescence of a Eu-doped Mg-Al layered double hydroxide (Eu-doped LDH) response to glutamic acid (Glu). Various characterizations (UV-Vis transmittance, TG-DTA and IR-spectrum) indicated that there is an interaction between the Eu-doped LDH and Glu. Fluorescent study was found that the red emissions resulted from (5)D(0)-(7)F(J) transition (J=1, 2) of Eu(3+) markedly decreased, while the blue emission at 440 nm contributed to Glu shifted to low energy after the addition of Glu to the Eu-doped LDH. The fluorescent changes may be relevant to the hydrogen-bond interaction between the Eu-doped LDH and Glu, and the mechanism of the interaction between Eu-doped LDH and Glu was discussed.
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PMID:Eu-doped Mg-Al layered double hydroxide as a responsive fluorescent material and its interaction with glutamic acid. 2295 9