4-hydroxyproline epimerase

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4-hydroxyproline epimerase
Identifiers
EC no. 5.1.1.8
CAS no. 9024-23-1
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BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
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In enzymology, a 4-hydroxyproline epimerase (EC 5.1.1.8) is an enzyme that catalyzes the chemical reaction

trans-4-hydroxy-L-proline cis-4-hydroxy-D-proline

Hence, this enzyme has one substrate, trans-4-hydroxy-L-proline, and one product, cis-4-hydroxy-D-proline.

This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is 4-hydroxyproline 2-epimerase. Other names in common use include hydroxyproline epimerase, hydroxyproline 2-epimerase, and L-hydroxyproline epimerase. This enzyme participates in arginine and proline metabolism.

Related Research Articles

Proline (symbol Pro or P) is an organic acid classed as a proteinogenic amino acid (used in the biosynthesis of proteins), although it does not contain the amino group -NH
2
but is rather a secondary amine. The secondary amine nitrogen is in the protonated form (NH2+) under biological conditions, while the carboxyl group is in the deprotonated −COO form. The "side chain" from the α carbon connects to the nitrogen forming a pyrrolidine loop, classifying it as a aliphatic amino acid. It is non-essential in humans, meaning the body can synthesize it from the non-essential amino acid L-glutamate. It is encoded by all the codons starting with CC (CCU, CCC, CCA, and CCG).

<span class="mw-page-title-main">Hydroxyproline</span> Chemical compound

(2S,4R)-4-Hydroxyproline, or L-hydroxyproline (C5H9O3N), is an amino acid, abbreviated as Hyp or O, e.g., in Protein Data Bank.

<span class="mw-page-title-main">Carotenoid</span> Class of chemical compounds; yellow, orange or red plant pigments

Carotenoids are yellow, orange, and red organic pigments that are produced by plants and algae, as well as several bacteria, archaea, and fungi. Carotenoids give the characteristic color to pumpkins, carrots, parsnips, corn, tomatoes, canaries, flamingos, salmon, lobster, shrimp, and daffodils. Over 1,100 identified carotenoids can be further categorized into two classes – xanthophylls and carotenes.

<span class="mw-page-title-main">Imino acid</span> Organic compound

In organic chemistry, an imino acid is any molecule that contains both imine (>C=NH) and carboxyl functional groups.

In chemistry, hydroxylation can refer to:

Isomerases are a general class of enzymes that convert a molecule from one isomer to another. Isomerases facilitate intramolecular rearrangements in which bonds are broken and formed. The general form of such a reaction is as follows:

A polyproline helix is a type of protein secondary structure which occurs in proteins comprising repeating proline residues. A left-handed polyproline II helix is formed when sequential residues all adopt (φ,ψ) backbone dihedral angles of roughly and have trans isomers of their peptide bonds. This PPII conformation is also common in proteins and polypeptides with other amino acids apart from proline. Similarly, a more compact right-handed polyproline I helix is formed when sequential residues all adopt (φ,ψ) backbone dihedral angles of roughly and have cis isomers of their peptide bonds. Of the twenty common naturally occurring amino acids, only proline is likely to adopt the cis isomer of the peptide bond, specifically the X-Pro peptide bond; steric and electronic factors heavily favor the trans isomer in most other peptide bonds. However, peptide bonds that replace proline with another N-substituted amino acid are also likely to adopt the cis isomer.

<span class="mw-page-title-main">Didemnin</span> Cyclic molecule found in tunicates

Didemnins are cyclic depsipeptide compounds isolated from a tunicate of the genus Trididemnum that were collected in the Caribbean Sea. They were first isolated in 1978 at the University of Illinois.

In enzymology, a 4-oxoproline reductase (EC 1.1.1.104) is an enzyme that catalyzes the chemical reaction

In enzymology, a procollagen-proline 3-dioxygenase (EC 1.14.11.7) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Procollagen-proline dioxygenase</span>

Procollagen-proline dioxygenase, commonly known as prolyl hydroxylase, is a member of the class of enzymes known as alpha-ketoglutarate-dependent hydroxylases. These enzymes catalyze the incorporation of oxygen into organic substrates through a mechanism that requires alpha-Ketoglutaric acid, Fe2+, and ascorbate. This particular enzyme catalyzes the formation of (2S, 4R)-4-hydroxyproline, a compound that represents the most prevalent post-translational modification in the human proteome.

In enzymology, a proline 3-hydroxylase (EC 1.14.11.28) is an enzyme that catalyzes the chemical reaction

In enzymology, a 1-pyrroline-5-carboxylate dehydrogenase (EC 1.2.1.88) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Pyrroline-5-carboxylate reductase</span>

In enzymology, a pyrroline-5-carboxylate reductase (EC 1.5.1.2) is an enzyme that catalyzes the chemical reaction

In enzymology, an aspartate racemase is an enzyme that catalyzes the following chemical reaction:

In enzymology, an isocitrate epimerase is classified as follows: EC 5.1.2.6. This number indicates that it is an isomerase, specifically a racemase or epimerase that acts on hydroxy acids and their derivatives, namely isocitrate. Isocitrate epimerase specifically catalyzes the reversible reaction:

In enzymology, a proline racemase is an enzyme that catalyzes the chemical reaction

The enzyme trans-L-3-hydroxyproline dehydratase (EC 4.2.1.77) catalyzes the chemical reaction

In enzymology, a 1-pyrroline-4-hydroxy-2-carboxylate deaminase (EC 3.5.4.22) is an enzyme that catalyzes the chemical reaction

References