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Titolo:
Crystal structure of thymidylate synthase A from Bacillus subtilis
Autore:
Fox, KM; Maley, F; Garibian, A; Changchien, LM; Van Roey, P;
Indirizzi:
New York State Dept Hlth, Wadsworth Ctr, Div Mol Med, Albany, NY 12201 USANew York State Dept Hlth Albany NY USA 12201 ol Med, Albany, NY 12201 USA Union Coll, Dept Chem, Schenectady, NY 12308 USA Union Coll Schenectady NY USA 12308 Dept Chem, Schenectady, NY 12308 USA
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 3, volume: 8, anno: 1999,
pagine: 538 - 544
SICI:
0961-8368(199903)8:3<538:CSOTSA>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
CATALYTIC MECHANISM; DIFFRACTION DATA; PHAGE PHI-3T; ACTIVE-SITE; 5-FLUORO-2'-DEOXYURIDYLATE; MACROMOLECULES; COMPLEX; PACKAGE; GENE;
Keywords:
Bacillus subtilis thymidylate synthase; structural comparison; ternary complex;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: Van Roey, P New2201k State Dept Hlth, Wadsworth Ctr, Div Mol Med, POB 509,Albany, NY 1 New York State Dept Hlth POB 509 Albany NY USA 12201 any, NY 1
Citazione:
K.M. Fox et al., "Crystal structure of thymidylate synthase A from Bacillus subtilis", PROTEIN SCI, 8(3), 1999, pp. 538-544

Abstract

Thymidylate synthase (TS) converts dUMP to dTMP by reductive methylation, where 5,10-methylenetetrahydrofolate is the source of both the methylene group and reducing equivalents. The mechanism of this reaction has been extensively studied, mainly using the enzyme from Escherichia coli. Bacillus subtilis contains two genes for TSs, ThyA and ThyB. The ThyB enzyme is very similar to other bacterial TSs, but the ThyA enzyme is quite different, birthin sequence and activity. In ThyA TS, the active site histidine is replaced by valine. In addition, the B. subtilis enzyme has a 2.4-fold greater k(cat) than the E. coli enzyme. The structure of B. subtilis thymidylate synthase in a ternary complex with 5-fluoro-dUMP and 5,10-methylenetetrahydrofolate has been determined to 2.5 Angstrom resolution. Overall, the structure of B. subtilis TS (ThyA) is similar to that of the E. coli enzyme. However,there are significant differences in the structures of two loops, the dimer interface and the details of the active site. The effects of the replacement of histidine by valine and a serine to glutamine substitution in the active site area, and the addition of a loop over the carboxy terminus may account for the differences in k(cat) found between the two enzymes.

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Documento generato il 29/11/20 alle ore 03:00:15