Pterin-4a-carbinolamine dehydratase from Pseudomonas aeruginosa: characterization, catalytic mechanism and comparison to the human enzyme.

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 Chem

journal_title

Biological chemistry

authors

Köster S,Stier G,Kubasch N,Curtius HC,Ghisla S

doi

10.1515/bchm.1998.379.12.1427

subject

Has Abstract

pub_date

1998-12-01 00:00:00

pages

1427-32

issue

12

eissn

1431-6730

issn

1437-4315

journal_volume

379

pub_type

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