期刊
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
卷 70, 期 1, 页码 157-166出版社
WILEY
DOI: 10.1002/prot.21622
关键词
multiple protein structural alignment; family-based approach; Aspergillus niger; Botrytis cinerea; plant petal death protein; lyase; gem-diol
资金
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM028688] Funding Source: NIH RePORTER
- NIGMS NIH HHS [GM28688] Funding Source: Medline
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.
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