The complete amino acid sequence of cytosolic serine hydroxymethyltransferase from rabbit liver and the partial sequence of mitochondrial isoenzyme were easily aligned with the cDNA-deduced sequence of E. coli enzyme. The homology within these three proteins in very high, whereas comparison with other PLP-enzymes, including the partially sequenced glutamate decarboxylase from E. coli, reveals only some homologies for restricted regions of the sequences.
Sequence studies on vitamin B6-dependent enzymes: serine hydroxymethyltransferase and glutamate decarboxylase / Bossa, Francesco; F., Martini; Angelaccio, Sebastiana; Pascarella, Stefano; Maras, Bruno; V., Schirch; Simmaco, Maurizio; R. A., John; Barra, Donatella. - STAMPA. - (1987), pp. 203-206. (Intervento presentato al convegno International Congress on Chemical and Biological Aspects of Vitamin B6 Catalysis tenutosi a Turku, Finlandia nel 22-26 giugno 1987).
Sequence studies on vitamin B6-dependent enzymes: serine hydroxymethyltransferase and glutamate decarboxylase
BOSSA, Francesco;ANGELACCIO, Sebastiana;PASCARELLA, Stefano;MARAS, Bruno;SIMMACO, Maurizio;BARRA, Donatella
1987
Abstract
The complete amino acid sequence of cytosolic serine hydroxymethyltransferase from rabbit liver and the partial sequence of mitochondrial isoenzyme were easily aligned with the cDNA-deduced sequence of E. coli enzyme. The homology within these three proteins in very high, whereas comparison with other PLP-enzymes, including the partially sequenced glutamate decarboxylase from E. coli, reveals only some homologies for restricted regions of the sequences.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
