Microsomally associated heme proteins from French bean: characterization of the cytochrome P450 cinnamate-4-hydroxylase and two peroxidases.

Abstract:

:Three heme-containing proteins of M(r) 57,000, 46,000, and 42,000 have been isolated from microsomes of elicitor-treated suspension-cultured cells of French bean. Following purification to homogeneity they were shown to be distinct with respect to amino acid and sugar compositions. The M(r) 57,000 protein proved to be the cytochrome P450 cinnamate-4-hydroxylase (CYP 73), by immunopurification and characterization. The M(r) 46,000 showed peroxidative activity toward guaiacol and all substituted phenylpropanoids tested and also gave a form of binding spectrum with cinnamic acid. The M(r) 42,000 had peroxidative activity toward guaiacol and a similar apparent binding spectrum to the M(r) 46,000 protein but was less active toward hydroxylated and methoxylated phenylpropanoids. The two peroxidases had cationic pIs and were distinct proteins rather than glycosylated or proteolytic variants.

journal_name

Arch Biochem Biophys

authors

Rodgers MW,Zimmerlin A,Werck-Reichhart D,Bolwell GP

doi

10.1006/abbi.1993.1323

subject

Has Abstract

pub_date

1993-07-01 00:00:00

pages

74-80

issue

1

eissn

0003-9861

issn

1096-0384

pii

S0003986183713238

journal_volume

304

pub_type

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