Abstract:
:The three-dimensional structure of pterin-4a-carbinolamine dehydratase (PCD) from Pseudomonas aeruginosa has been solved. Based on this we have investigated the roles of putative active center residues through functional replacement by site-directed mutagenesis. Three histidines, His73, His74 and His91, appear to be involved in dehydration catalysis. The three-dimensional positions of these residues match those of corresponding histidines at the active center of human PCD. Based on the coincidence of catalytic parameters, and on the similar effects induced by the mutations, it is concluded that the substrate binding mode and the reaction mechanisms of bacterial and human PCD are basically identical.
journal_name
Biol Chemjournal_title
Biological chemistryauthors
Köster S,Stier G,Kubasch N,Curtius HC,Ghisla Sdoi
10.1515/bchm.1998.379.12.1427subject
Has Abstractpub_date
1998-12-01 00:00:00pages
1427-32issue
12eissn
1431-6730issn
1437-4315journal_volume
379pub_type
杂志文章abstract::Bacterial proteases secreted into an infected host may exhibit a wide range of pathogenic potentials. Staphylococci, in particular Staphylococcus aureus, are known to produce several extracellular proteases, including serine-, cysteine- and metalloenzymes. Their insensitivity to most human plasma protease inhibitors a...
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journal_title:Biological chemistry
pub_type: 杂志文章
doi:
更新日期:1998-04-01 00:00:00