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来自青霉素产生菌产黄青霉的锰超氧化物歧化酶。

The manganese superoxide dismutase from the penicillin producer Penicillium chrysogenum.

作者信息

Díez B, Schleissner C, Moreno M A, Rodríguez M, Collados A, Barredo J L

机构信息

Laboratorios de Ingeniería Genética and Bioquímica Antibióticos S. A., Avendida de Antibióticos 59 - 61, E-24080 León, Spain.

出版信息

Curr Genet. 1998 Jun;33(6):387-94. doi: 10.1007/s002940050351.

DOI:10.1007/s002940050351
PMID:9644201
Abstract

The antioxidant enzyme superoxide dismutase has been studied in order to define mechanisms for the influence of oxygen on penicillin production. Manganese-containing SOD activity was purified from penicillin-producing cultures of the filamentous fungus Penicillium chrysogenum and reverse genetics was used to identify full-length cDNA and genomic clones. Sequence analysis revealed a 630-bp ORF containing three exons and two introns with fungal consensus splice-site junctions. The deduced amino-acid sequence (210 amino acids; 23.13 kDa) includes conserved residues required for enzymatic activity and metal binding, and shares significant similarity with Mn- and Fe-containing superoxide dismutases. The sod gene is present as a single copy in the genome of different P. chrysogenum strains and its expression level is not correlated with penicillin-G productivity.

摘要

为了确定氧气对青霉素生产影响的机制,对抗氧化酶超氧化物歧化酶进行了研究。从产黄青霉丝状真菌的青霉素生产培养物中纯化了含锰的超氧化物歧化酶活性,并利用反向遗传学鉴定全长cDNA和基因组克隆。序列分析显示一个630bp的开放阅读框,包含三个外显子和两个内含子,具有真菌共有剪接位点连接。推导的氨基酸序列(210个氨基酸;23.13 kDa)包括酶活性和金属结合所需的保守残基,并且与含锰和含铁的超氧化物歧化酶具有显著相似性。超氧化物歧化酶基因在不同产黄青霉菌株的基因组中以单拷贝形式存在,其表达水平与青霉素G的生产力无关。

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