Hydroxylation of (Pro-Pro-Gly)5 and (Pro-Pro-Gly)10 by prolyl hydroxylase. Evidence for an asymmetric active site in the enzyme.
Berg, R A
Hydroxylation of (Pro-Pro-Gly)5 and (Pro-Pro-Gly)10 by prolyl hydroxylase. Evidence for an asymmetric active site in the enzyme. [electronic resource] - Biochemistry Apr 1977 - 1615-21 p. digital
Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.
0006-2960
10.1021/bi00627a014 doi
Amino Acid Sequence
Animals
Binding Sites
Chick Embryo
Glycine
Kinetics
Peptide Biosynthesis
Procollagen-Proline Dioxygenase--isolation & purification
Proline
Structure-Activity Relationship
Hydroxylation of (Pro-Pro-Gly)5 and (Pro-Pro-Gly)10 by prolyl hydroxylase. Evidence for an asymmetric active site in the enzyme. [electronic resource] - Biochemistry Apr 1977 - 1615-21 p. digital
Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.
0006-2960
10.1021/bi00627a014 doi
Amino Acid Sequence
Animals
Binding Sites
Chick Embryo
Glycine
Kinetics
Peptide Biosynthesis
Procollagen-Proline Dioxygenase--isolation & purification
Proline
Structure-Activity Relationship