Conformational requirement for lysine hydroxylation in collagen. Structural studies on synthetic peptide substrates of lysyl hydroxylase.
نویسندگان
چکیده
منابع مشابه
Structural studies on peptide binding domain of human type I collagen prolyl 4-hydroxylase
Collagen prolyl 4-hydroxylase (C-P4H) catalyses the formation of 4-hydroxyproline in collagens. Hydroxylation of prolines in –X-Pro-Glysequences is necessary for the formation of stable collagen triple helices. Molecular oxygen, Fe, 2-oxogluterate and ascorbate are required for the reaction [1]. In vertebrates C-P4H is an 2 2 tetramer in which is the catalytic subunit and the subunit is identic...
متن کاملImmunological characterization of lysyl hydroxylase, an enzyme of collagen synthesis.
Antibodies to pure lysyl hydroxylase from whole chick embryos were prepared in rabbits and used for immunological characterization of this enzyme of collagen biosynthesis. In double immunodiffusion a single precipitation line was seen between the antiserum and crude or pure chick-embryo lysyl hydroxylase. The antiserum effectively inhibited chick-embryo lysyl hydroxylase activity, whether measu...
متن کاملConformational implications of enzymatic proline hydroxylation in collagen.
In 1979 it was proposed that prolyl hydroxylase (prolyl-glycyl-peptide,2-oxoglutarate:oxygen oxidoreductase, EC 1.14.11.2) recognizes the beta-turn conformation in nascent procollagen chains and that the hydroxylation process involves a conformational change resulting in "straightening" of the beta-turn segments into the linear triple-helical conformation of native collagen. We present experime...
متن کاملConformational preferences of substrates for human prolyl 4-hydroxylase.
Prolyl 4-hydroxylase (P4H) catalyzes the posttranslational hydroxylation of (2 S)-proline (Pro) residues in procollagen strands. The resulting (2 S,4 R)-4-hydroxyproline (Hyp) residues are essential for the folding, secretion, and stability of the collagen triple helix. Even though its product (Hyp) differs from its substrate (Pro) by only a single oxygen atom, no product inhibition has been ob...
متن کاملInherited human collagen lysyl hydroxylase deficiency: ascorbic acid response.
A patient is described with congenital hypotonia, lax joints, friable skin, hemorrhagic scars, high-arched palate, and borderline microcornea. Acid hydrolyzed whole skin collagen had a reduced hydroxylysine content of 0.5 residues per 1,000 as compared to 5.1 +/- 0.7 in control skin. Collagen lysyl hydroxylase in dialyzed subcellular fractions of cultured skin fibroblasts required L-ascorbate a...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1991
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)54448-3