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1 10-
Formyltetrahydrofolate dehydrogenase (
10-FTHFDH) is a fo
2 We conclude that the 10-
formyltetrahydrofolate dehydrogenase activity of FDH is
3 th alanines resulted in total loss of the 10-
formyltetrahydrofolate dehydrogenase activity, whereas t
4 ctivity, and the full-length FDH produces 10-
formyltetrahydrofolate dehydrogenase activity.
5 zyme catalytic centers but is crucial for 10-
formyltetrahydrofolate dehydrogenase activity.
6 viously purified COOH-terminal domain had 10-
formyltetrahydrofolate dehydrogenase activity.
7 ALDH1L1 (10-
formyltetrahydrofolate dehydrogenase),
an enzyme of fola
8 rity between the amino-terminal domain of 10-
formyltetrahydrofolate dehydrogenase and methionyl-tRNA-
9 Passage of a reaction mixture of 10-
formyltetrahydrofolate dehydrogenase down a size exclusi
10 e model have shown a crucial role for the 10-
formyltetrahydrofolate dehydrogenase enzyme in serine-to
11 The liver cytosolic enzyme, 10-
formyltetrahydrofolate dehydrogenase (
FDH) (EC 1.5.1.6)
12 10-
Formyltetrahydrofolate dehydrogenase (
FDH) catalyzes an
13 The enzyme 10-
formyltetrahydrofolate dehydrogenase (
FDH) catalyzes con
14 10-
Formyltetrahydrofolate dehydrogenase (
FDH) catalyzes the
15 10-
Formyltetrahydrofolate dehydrogenase (
FDH) consists of t
16 10-
Formyltetrahydrofolate dehydrogenase (
FDH) converts 10-f
17 10-
Formyltetrahydrofolate dehydrogenase (
FDH) is composed o
18 s identified as an additional activity of 10-
formyltetrahydrofolate dehydrogenase (
FDH) protein.
19 The enzyme, 10-
formyltetrahydrofolate dehydrogenase (
FDH), converts 10-
20 one of the enzymes of folate metabolism, 10-
formyltetrahydrofolate dehydrogenase (
FDH), requires a 4
21 the multidomain, multifunctional enzyme, 10-
formyltetrahydrofolate dehydrogenase (
FDH), using a bacu
22 The C-terminal domain (C(t)-FDH) of 10-
formyltetrahydrofolate dehydrogenase (
FDH, ALDH1L1) is a
23 Cytosolic 10-
formyltetrahydrofolate dehydrogenase (
FDH, ALDH1L1) is a
24 10-
Formyltetrahydrofolate dehydrogenase is also known to ex
25 FDH (10-
formyltetrahydrofolate dehydrogenase)
is strongly downre
26 Coupling the 10-
formyltetrahydrofolate dehydrogenase reaction to an exce
27 A new rapid procedure for purifying 10-
formyltetrahydrofolate dehydrogenase results in 90 mg of
28 lysis of the product inhibition curve for 10-
formyltetrahydrofolate dehydrogenase shows that H4-PteGl
29 There is a several-fold excess of 10-
formyltetrahydrofolate dehydrogenase subunits in liver r
30 ependent crystallographic support in work on
formyltetrahydrofolate dehydrogenase,
work which further