Prolyl 4-hydroxylases catalyze the formation of 4-hydroxyproline in collagens and other proteins with an appropriate collagen-like stretch of amino acid residues. The enzyme requires Fe(II), 2-oxoglutarate, molecular oxygen, and ascorbate. This review concentrates on recent progress toward understanding the detailed mechanism of 4-hydroxylase action, including: (a) occurrence and function of the enzyme in animals; (b) general molecular properties; (c) intracellular sites of hydroxylation; (d) peptide substrates and mechanistic roles of the cosubstrates; (e) insights into the development of antifibrotic drugs; (f) studies of the enzyme's subunits and their catalytic function; and (g) mutations that lead to Ehlers-Danlos Syndrome. An account of the regulation of collagen hydroxylase activities is also provided.

Collagen Hydroxylases and the Protein Disulfide Isomerase Subunit of Prolyl 4‐Hydroxylases

Non-proteinogenic prolines have been acknowledged as an important pool for the synthesis of conformationally rigid bioactive peptides, angiotensin converting enzyme inhibitors and as pharmacological probes. Proline and its derivatives are often used as asymmetric catalysts in organic reactions, such as CBS reductions and proline catalyzed aldol reactions, Mannich reactions, and so on. Furthermore l -proline is an osmoprotectant and is therefore frequently used in many pharmacological as well as biotechnological applications. The wide range of chemical and biological applications associated with l -proline has prompted researchers to develop new methodologies for the synthesis of prolines and substituted prolines and to further explore their chemical and biological applications. The present article is an attempt to discuss all the major advances available till date, describing the use of proline in organic asymmetric synthesis, the synthesis of various bioactive molecules or proline as a constituent part of bioactive molecules.

Advances in the chemistry of proline and its derivatives: an excellent amino acid with versatile applications in asymmetric synthesis

Recently, the importance of proline ring pucker conformations in collagen has been suggested in the context of hydroxylation of prolines The previous molecular mechanics parameters for hydroxyproline, however, do not reproduce the correct pucker preference We have developed a new set of parameters that reproduces the correct pucker preference Our molecular dynamics simulations of proline and hydroxyproline monomers as well as collagen-like peptides, using the new parameters, support the theory that the role of hydroxylation in collagen is to stabilize the triple helix by adjusting to the right pucker conformation (and thus the right ϕ angle) in the Y position © 2005 Wiley Periodicals, Inc J Comput Chem 26: 1612–1616, 2005

A new set of molecular mechanics parameters for hydroxyproline and its use in molecular dynamics simulations of collagen‐like peptides

An evaluation of [3‘-(2-aminoethyl)-2-biphenyl]propionic acid (1) and 2-amino-3‘-biphenylcarboxylic acid (2) as β-sheet nucleators was accomplished by incorporating these residues into water solubl

A 2,3‘-Substituted Biphenyl-Based Amino Acid Facilitates the Formation of a Monomeric β-Hairpin-like Structure in Aqueous Solution at Elevated Temperature

/pdf/protein-structure-and-function-from-a-colloidal-to-a-1t1d4qfdqn.pdf

Protein structure and function, from a colloidal to a molecular view

Conformational-energy computations have been carried out for the N-acetyl-N′-methylamides of the Pro-Pro, Pro-Gly, and Gly-Pro dipeptides and of the Pro-Pro-Gly-Pro tetrapeptide, serving as models for the conformational analysis of single-stranded poly(Gly-Pro-Pro). The probability of β-bend formation for the Pro-Gly sequence is very high, viz., 0.72 for the terminally blocked Pro-Gly dipeptide, and rises to 0.86 in the tetrapeptide. The β-bend conformations of the Pro-Gly sequence are of low energy in single-chain poly(Gly-Pro-Pro) as well. The β-bend structure had been postulated earlier to be a requirement for post-translational proline hydroxylation during the biosynthesis of collagen. The present results lend strong support to this proposal by demonstrating that the β-bend structure is energetically favorable and hence can be accommodated easily in single-stranded poly(Gly-Pro-Pro).

β‐Bend conformation of CH3CO‐Pro‐Pro‐Gly‐Pro‐NHCH3: Implications for posttranslational proline hydroxylation in collagen

A matrix formulation of the conformational partition function is used to assess the influence of irregular structures on the formation of intramolecular antiparallel β sheets. An antiparallel sheet is considered to be irregular if any pair of contiguous strands has an unequal number of residues. The regular structures in the model consist of antiparallel sheets in which every strand contains the same number of residues. Aside from a growth parameter t, the model contains two parameters that account for the influence of edge effects. Each tight turn contributes a factor δ, and each residue in the sheet that does not have a partner in a preceding strand contributes a factor τ. When τ < δ = 1, preferred sheets consist of an extremely large number of very short strands. Such sheets resemble those found in cross-β fibers. Irregular structures increase the cooperativity of the formation of cross-β fibers. They cause the fibers that are formed to be longer (have more strands) and thicker (have more residues per ...

Dominance of irregular structures in the formation of intramolecular antiparallel β sheets by homopolyamino acids

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β‐Bend conformation of CH3CO‐Pro‐Pro‐Gly‐Pro‐NHCH3: Implications for posttranslational proline hydroxylation in collagen

Dominance of irregular structures in the formation of intramolecular antiparallel β sheets by homopolyamino acids