THE PGR1 MUTANT OF COCHLIOBOLUS-HETEROSTROPHUS LACKS A P-DIPHENOL OXIDASE INVOLVED IN NAPHTHALENEDIOL MELANIN SYNTHESIS

被引:23
作者
TANAKA, C [1 ]
TAJIMA, S [1 ]
FURUSAWA, I [1 ]
TSUDA, M [1 ]
机构
[1] KYOTO UNIV, FAC AGR, PLANT PATHOL LAB, KYOTO 606, JAPAN
来源
MYCOLOGICAL RESEARCH | 1992年 / 96卷
关键词
D O I
10.1016/S0953-7562(09)80598-4
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
1,8-Dihydroxynaphthalene (1,8-DHN) was isolated from Cochliobolus heterostrophus pale green mutant M13BL19 (Alb1+ Brn1+ Sal1+ Pgr1-1) as the active substance which restored melanization of HE1AS73 (Alb1-8 Brn1-2 Sal1-1 Pgr1+). HE1AS73 oxidized 1,8-DHN, 1-naphthol, N,N-dimethyl-p-phenylenediamine, tetramethylbenzidine, syringaldazine, and 3-(3,4-dihydroxyphenyl)alanine, but did not oxidize p-cresol and L-tyrosine. None of these compounds was oxidized by HE5R13 (Alb1-8 Brn1-2 Sal1-1 Pgr1-1). The syringaldazine oxidation activity of HE1AS73 was inhibited by diethyldithiocarbamate, cetyltrimethylammonium bromide, and dithiopyrimidine. These results indicate that the Pgr1+ strain contained p-diphenol oxidase which was absent from the Pgr1- strain. We consider from these results that p-diphenol oxidase, in which Pgr1 is involved, plays a role in melanin synthesis of C. heterostrophus and 1,8-DHN is a natural substrate of this enzyme.
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页码:959 / 964
页数:6
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