PMID:3060113
| Citation |
Vasudevan, SG, Shaw, DC and Armarego, WL (1988) Dihydropteridine reductase from Escherichia coli. Biochem. J. 255:581-8 |
|---|---|
| Abstract |
A dihydropteridine reductase from Escherichia coli was purified to apparent homogeneity. It is a dimeric enzyme with identical subunits (Mr 27000) and a free N-terminal group. It can use NADH (Vmax./Km 3.36 s-1) and NADPH (Vmax./Km 1.07 s-1) when 6-methyldihydro-(6H)-pterin is the second substrate, as well as quinonoid dihydro-(6H)-biopterin (Vmax./Km 0.69 s-1), dihydro-(6H)-neopterin (Vmax./Km 0.58 s-1), dihydro-(6H)-monapterin 0.66 s-1), 6-methyldihydro-(6H)-pterin and cis-6,7-dimethyldihydro-(6H)-pterin (Vmax./Km 0.66 s-1) when NADH is the second substrate. The pure reductase has a yellow colour and contains bound FAD. The enzyme also has pterin-independent NADH and NADPH oxidoreductase activities when potassium ferricyanide is the electron acceptor. |
| Links | |
| Keywords |
Amino Acid Sequence; Chromatography, Ion Exchange; Dihydropteridine Reductase/isolation & purification; Dihydropteridine Reductase/metabolism; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology; Flavin-Adenine Dinucleotide/metabolism; Kinetics; Methotrexate/pharmacology; Molecular Sequence Data; Molecular Weight; NAD/metabolism; NADH, NADPH Oxidoreductases/metabolism; Spectrophotometry, Ultraviolet; Substrate Specificity |
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