Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
SITE-DIRECTED MUTAGENESIS AND STEADY-STATE KINETIC-ANALYSIS OF MUTANTENZYMES OF HUMAN ADENYLATE KINASE
Autore:
AYABE T; PARK SK; NAGAHAMA H; MARUYAMA H; SUMIDA M; TAKENAKA H; TAKENAKA O; ONITSUKA T; HAMADA M;
Indirizzi:
MIYAZAKI MED COLL,DEPT HYG MIYAZAKI 8891692 JAPAN MIYAZAKI MED COLL,DEPT HYG MIYAZAKI 8891692 JAPAN MIYAZAKI MED COLL,DEPT SURG 2 MIYAZAKI 8891692 JAPAN EHIME UNIV,SCH MED,DEPT SECOND MED BIOCHEM SHIGENOBU EHIME 79102 JAPAN KYOTO UNIV,PRIMATE RES INST INUYAMA AICHI 484 JAPAN
Titolo Testata:
Biochemistry and molecular biology international
fascicolo: 4, volume: 46, anno: 1998,
pagine: 673 - 680
SICI:
1039-9712(1998)46:4<673:SMASKO>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
ADENOSINE-TRIPHOSPHATE TRANSPHOSPHORYLASES; ATP-AMP TRANSPHOSPHORYLASE; BINDING-SITE; CRYSTALLINE RABBIT; CALF MUSCLE; RESIDUES;
Keywords:
ADENYLATE KINASE; SITE-DIRECTED MUTAGENESIS; STEADY-STATE KINETICS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
22
Recensione:
Indirizzi per estratti:
Citazione:
T. Ayabe et al., "SITE-DIRECTED MUTAGENESIS AND STEADY-STATE KINETIC-ANALYSIS OF MUTANTENZYMES OF HUMAN ADENYLATE KINASE", Biochemistry and molecular biology international, 46(4), 1998, pp. 673-680

Abstract

Site-directed mutagenesis of human adenylate kinase (AK) was carried out on residues His36, Lys55, and the C-terminal segment (Val182, V186, and Leu193). Five mutants {(H36T, K55G, V182G, V186S, and L193Stop (deletion of residues 193-194)} were generated and analyzed by steady state kinetics. H36T, K55G, and L193Stop mutants showed an increase of K-m values (19.8-, 19.7-, and 11.3-fold) for AMP(2-) compared to that for the wild-type enzyme, and these residues appeared to interact withAMP(2-). V182G showed an increased K-m value (7.4-fold) for MgATP(2-). Therefore, V182 may be essential for interaction with MgATP2-. V186Sincreased the K-m value (7.0- and 7.5-fold) for MgATP2- and AMP2-. V186 may thus interact with both substrates. The C-terminal domain of AKappears to be essential for MgATP2- and AMP(2-) binding.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/07/20 alle ore 10:23:32