Purification and Characterization of Cob(II)yrinic Acid A,c-diamide Reductase from Pseudomonas Denitrificans
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An NADH-dependent flavoenzyme exhibiting cob(II)yrinic acid a,c-diamide reductase activity was purified 6,300-fold to homogeneity from Pseudomonas denitrificans and sequenced at its N terminus. This enzyme of the cobalamin biosynthetic pathway reduced to the Co(I) state all of the Co(II)-corrinoids isolated from this microorganism.
Exploring Bacterial Microcompartments in the Acetogenic Bacterium .
Chowdhury N, Alberti L, Linder M, Muller V Front Microbiol. 2020; 11:593467.
PMID: 33178174 PMC: 7593272. DOI: 10.3389/fmicb.2020.593467.
Metabolic engineering of Escherichia coli for de novo biosynthesis of vitamin B.
Fang H, Li D, Kang J, Jiang P, Sun J, Zhang D Nat Commun. 2018; 9(1):4917.
PMID: 30464241 PMC: 6249242. DOI: 10.1038/s41467-018-07412-6.
FAD binding, cobinamide binding and active site communication in the corrin reductase (CobR).
Lawrence A, Taylor S, Scott A, Rowe M, Johnson C, Rigby S Biosci Rep. 2014; 34(4).
PMID: 24909839 PMC: 4083273. DOI: 10.1042/BSR20140060.
Parsons J, Lawrence A, McLean K, Munro A, Rigby S, Warren M PLoS One. 2010; 5(11):e14009.
PMID: 21103360 PMC: 2982820. DOI: 10.1371/journal.pone.0014009.
Reduction of Cob(III)alamin to Cob(II)alamin in Salmonella enterica serovar typhimurium LT2.
Fonseca M, Escalante-Semerena J J Bacteriol. 2000; 182(15):4304-9.
PMID: 10894741 PMC: 101946. DOI: 10.1128/JB.182.15.4304-4309.2000.