| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 7772176 | Bioorganic Chemistry | 2012 | 9 Pages |
Abstract
⺠Ornithine 4,5 aminomutase is a PLP and adenosylcobalamin-dependent radical enzyme. ⺠Active site His225 forms a hydrogen bond to PLP phenolic oxygen. ⺠H225A and H225Q mutants have lower rates of catalytic turnover and specificity. ⺠His225 contributes to the overstabilization of PLP radical intermediates. ⺠His225 potentially participates in catalysis by partial proton transfer to PLP.
Keywords
NTA2-morpholinoethanesulfonic acid monohydrateDAPDHlysine 5,6-aminomutaseOAMAdoCblEPPSCHESTRISTIMTriosephosphate isomeraseHEPESDAPPLPAEBSF4-(2-aminoethyl) benzenesulfonyl fluoride hydrochlorideN-(2-Hydroxyethyl)piperazine-N′-2-ethanesulfonic acidNAD+β-nicotinamide adenine dinucleotideAdenosylcobalamin2,4-Diaminobutyric acidnitrilotriacetic acidSDS-PAGESodium dodecyl sulfate polyacrylamide gel electrophoresisTris(hydroxymethyl)aminomethaneDabaMeSpyridoxal 5′-phosphate
Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Caitlyn Makins, François N. Miros, Nigel S. Scrutton, Kirsten R. Wolthers,