Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxygenase1.
The catechol dioxygenases allow a wide variety of bacteria to use aromatic compounds as carbon sources by catalyzing the key ring-opening step. These enzymes use specifically either catechol or protocatechuate (2,3-dihydroxybenozate) as their substrates; they use a bare metal ion as the sole cofactor. To learn how this family of metalloenzymes functions, a structural analysis of designed and selected mutants of these enzymes has been undertaken. Here we review the results of this analysis on the nonheme ferric iron intradiol dioxygenase protocatechuate 3,4-dioxygenase.
Brown
C Kent
CK
Center for Metals in Biocatalysis and Department of Biochemistry, Molecular Biology, and Biophysics , Minneapolis, Minnesota 55455, USA. brow0927@umn.edu
Vetting
Matthew W
MW
Earhart
Cathleen A
CA
Ohlendorf
Douglas H
DH
D000150:Acinetobacter / Q000201:enzymology; D000595:Amino Acid Sequence; D002396:Catechols / Q000378:metabolism*; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017354:Point Mutation; D011487:Protein Conformation; D011520:Protocatechuate-3,4-Dioxygenase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011549:Pseudomonas / Q000201:enzymology; D016415:Sequence Alignment
D002396:Catechols; D011520:Protocatechuate-3,4-Dioxygenase