Conformation and interaction of phenylalanine with the divalent cation at the active site of human recombinant tyrosine hydroxylase as determined by proton NMR-Reference-Cited by-同舟云学术

Conformation and interaction of phenylalanine with the divalent cation at the active site of human recombinant tyrosine hydroxylase as determined by proton NMR

Published:1993-06-29 Issue:25 Volume:32 Page:6381-6390
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Martinez Aurora,Abeygunawardana Chitrananda,Haavik Jan,Flatmark Torgeir,Mildvan Albert S.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00076a011

Reference49 articles.

1. Neutron diffraction study of L-phenylalanine hydrochloride

2. Regulation of recombinant human tyrosine hydroxylase isozymes by catecholamine binding and phosphorylation. Structure/activity studies and mechanistic implications

3. Resonance Raman studies on the blue-green-colored bovine adrenal tyrosine 3-monooxygenase (tyrosine hydroxylase). Evidence that the feedback inhibitors adrenaline and noradrenaline are coordinated to iron.

4. Evidence from EPR spectroscopy that phosphorylation of Ser-40 in bovine adrenal tyrosine hydroxylase facilitates the reduction of high-spin Fe(III) under turnover conditions

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