The active site of deoxyhypusyl hydroxylase: use of catecholpeptides and their component chelator and peptide moieties as molecular probes

Protein hydroxylation: prolyl 4‐hydroxylase, an enzyme with four cosubstrates and a multifunctional subunit

Kari I. Kivirikko, Raili Myllylä, Taina Pihlajaniemi · The FASEB Journal · 1989 · 320 citations

Life Sciences, Biochemistry, Molecular Biology +16

Coordination chemistry of microbial iron transport compounds. 9. Stability constants for catechol models of enterobactin

Alex Avdeef, Stephen R. Sofen, Thomas L. Bregante et al. · Journal of the American Chemical Society · 1978 · 308 citations

Life Sciences, Microbiology, Biological Transport Phenomena +10

Coordination chemistry of microbial iron transport compounds. 19. Stability constants and electrochemical behavior of ferric enterobactin and model complexes

Wesley R. Harris, Carl J. Carrano, Stephen R. Cooper et al. · Journal of the American Chemical Society · 1979 · 291 citations

Natural Sciences, Biochemistry, Chemistry +13

A stereochemical concept for the catalytic mechanism of prolylhydroxylase

Hartmut M. Hanauske‐Abel, Volkmar Günzler · Journal of Theoretical Biology · 1982 · 268 citations

Life Sciences, Biochemistry, Chemistry +14

The biosynthesis of protein-bound hypusine (N epsilon -(4-amino-2-hydroxybutyl)lysine). Lysine as the amino acid precursor and the intermediate role of deoxyhypusine (N epsilon -(4-aminobutyl)lysine).

M H Park, Herbert L. Cooper, J.E. Folk · Journal of Biological Chemistry · 1982 · 154 citations · Full text

Life Sciences, Biochemistry, Molecular Biology +16