Identification of fungal oxaloacetate hydrolyase within the isocitrate lyase/PEP mutase enzyme superfamily using a sequence marker-based method

被引：25

作者：

Joosten, Henk-Jan ^{[1
]}

Han, Ying ^{[2
]}

Niu, Weiling ^{[2
]}

Vervoort, Jacques ^{[3
]}

Dunaway-Mariano, Debra ^{[2
]}

Schaap, Peter J. ^{[1
]}

机构：

[1] Wageningen Univ, Microbiol Lab, NL-6703 AA Wageningen, Netherlands

[2] Univ New Mexico, Dept Chem, Albuquerque, NM 87131 USA

[3] Wageningen Univ, Biochem Lab, NL-6703 AA Wageningen, Netherlands

来源：

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 2008年 / 70卷 / 01期

关键词：

multiple protein structural alignment; family-based approach; Aspergillus niger; Botrytis cinerea; plant petal death protein; lyase; gem-diol;

D O I：

10.1002/prot.21622

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Aspergillus niger produces oxalic acid through the hydrolysis of oxaloacetate, catalyzed by the cytoplasmic enzyme oxaloacetate acetylhydrolase (OAH). The A. niger genome encodes four additional open reading frames with strong sequence similarity to OAH yet only the oahA gene encodes OAH activity. OAH and OAH-like proteins form subclass of the isocitrate lyase/PEP mutase enzyme superfamily, which is ubiquitous present filamentous fungi. Analysis of function-specific residues using a superfamily-based approach revealed an active site serine as a possible sequence marker for OAH activity. We propose that presence of this serine in family members correlates with presence of OAH activity whereas its absence correlates with absence of OAH. This hypothesis was tested by carrying out a serine mutagenesis study with the OAH from the fungal oxalic acid producer Botrytis cinerea and the OAH active plant petal death protein as test systems.

引用

页码：157 / 166

页数：10

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