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Titolo:
REGULATION OF N-TERMINUS-DELETED HUMAN TYROSINE-HYDROXYLASE TYPE-1 BYEND-PRODUCTS OF CATECHOLAMINE BIOSYNTHETIC-PATHWAY
Autore:
OTA A; YOSHIDA S; NAGATSU T;
Indirizzi:
FUJITA HLTH UNIV,SCH MED,INST COMPREHENS MED SCI,JOINT RES DIV THERAPIES INTRACTABLE DIS TOYOAKE AICHI 47011 JAPAN FUJITA HLTH UNIV,SCH MED,INST COMPREHENS MED SCI,JOINT RES DIV THERAPIES INTRACTABLE DIS TOYOAKE AICHI 47011 JAPAN FUJITA HLTH UNIV,SCH MED,INST COMPREHENS MED SCI,DIV MOL GENET NEUROCHEM 2 TOYOAKE AICHI 47011 JAPAN
Titolo Testata:
Journal of neural transmission
fascicolo: 12, volume: 103, anno: 1996,
pagine: 1415 - 1428
SICI:
0300-9564(1996)103:12<1415:RONHTT>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
BOVINE ADRENAL-MEDULLA; MESSENGER-RNA; KINETIC-PROPERTIES; ENZYME-ACTIVITY; SINGLE GENE; CDNA CLONE; BINDING; MUTAGENESIS; COFACTOR; 3-MONOOXYGENASE;
Keywords:
TYROSINE HYDROXYLASE; DELETION MUTAGENESIS; CATECHOLAMINE; TETRAHYDROBIOPTERIN; EXPRESSION IN ESCHERICHIA COLI;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
37
Recensione:
Indirizzi per estratti:
Citazione:
A. Ota et al., "REGULATION OF N-TERMINUS-DELETED HUMAN TYROSINE-HYDROXYLASE TYPE-1 BYEND-PRODUCTS OF CATECHOLAMINE BIOSYNTHETIC-PATHWAY", Journal of neural transmission, 103(12), 1996, pp. 1415-1428

Abstract

The N-terminal 52-, 70-, and 157-amino acids-deleted mutants and wild-type tyrosine hydroxylases were expressed in Escherichia coli and utilized to investigate the roles of the N-terminus in the catecholamine inhibition on enzyme activity. Their lysate's supernatants were used as enzyme samples. Three catecholamines, namely dopamine, norepinephrine, and epinephrine, affected both wild-type and mutant enzymes after preincubation in the mode of mixed inhibition, and the most marked alteration among the kinetic parameters produced by the deletion was the increase in the inhibition constants. The deletions also abolished the catecholamine-induced shift of the pH profile of the enzyme activity toward a more acidic pH optimum. All three mutants responded to catecholamines almost in the same way. These results suggest that the three catecholamine end products exert their inhibition on tyrosine hydroxylase to the same extent and that the N-terminal 52 amino acid residues contain the key sequence in mediating the inhibitory action.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/04/20 alle ore 13:16:13