Aliphatic (1)H, (13)C and (15)N chemical shift assignments of dihydrofolate reductase from the psychropiezophile Moritella profunda in complex with NADP(+) and folate.

Authors :: Loveridge EJ
Matthews SM
Williams C
Whittaker SB
Günther UL
Evans RM
Dawson WM
Crump MP
Allemann RK
Source :: Biomolecular NMR assignments [Biomol NMR Assign] 2013 Apr; Vol. 7 (1), pp. 61-4. Date of Electronic Publication: 2012 Mar 14.
Publication Year :: 2013
Abstract: Dihydrofolate reductase from the deep-sea bacterium Moritella profunda (MpDHFR) has been (13)C/(15)N isotopically labelled and purified. Here, we report the aliphatic (1)H, (13)C and (15)N resonance assignments of MpDHFR in complex with NADP(+) and folate. The spectra of MpDHFR suggest considerably greater conformational heterogeneity than is seen in the closely related DHFR from Escherichia coli.

Subjects :: Folic Acid metabolism
Moritella enzymology
NADP metabolism
Nuclear Magnetic Resonance, Biomolecular
Tetrahydrofolate Dehydrogenase chemistry
Tetrahydrofolate Dehydrogenase metabolism

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