Search results
Results from the WOW.Com Content Network
The most obvious, first effects (gingival and hair problems) of absence of ascorbic acid in humans come from the resulting defect in hydroxylation of proline residues of collagen, with reduced stability of the collagen molecule, causing scurvy. Increased serum and urine levels of hydroxyproline have also been demonstrated in Paget's disease. [10]
Procollagen-proline dioxygenase catalyzes the following reaction: L-proline + alpha-ketoglutaric acid + O 2 → (2S, 4R)-4-hydroxyproline + succinate + CO 2. The mechanism for the reaction is similar to that of other dioxygenases, and occurs in two distinct stages: [3] In the first, a highly reactive Fe(IV)=O species is produced.
As of 2011, 28 types of human collagen have been identified, described, and classified according to their structure. [8] This diversity shows collagen's diverse functionality. [9] All of the types contain at least one triple helix. [8] Over 90% of the collagen in humans is type I & III collagen. [10] Fibrillar (type I, II, III, V, XI) Non-fibrillar
1281 12825 Ensembl ENSG00000168542 ENSMUSG00000026043 UniProt P02461 P08121 RefSeq (mRNA) NM_000090 NM_001376916 NM_009930 RefSeq (protein) NP_000081 NP_034060 Location (UCSC) Chr 2: 188.97 – 189.01 Mb Chr 1: 45.35 – 45.39 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Type III Collagen is a homotrimer, or a protein composed of three identical peptide chains (monomers), each ...
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). Proline is the only proteinogenic amino acid which is a secondary amine , as the nitrogen atom is attached both to the α-carbon and to a chain of three ...
Hydroxylation improves water‐solubility, as well as affecting their structure and function. The most frequently hydroxylated amino acid residue in human proteins is proline . This is because collagen makes up about 25–35% of the protein in our bodies and contains a hydroxyproline at almost every 3rd residue in its amino acid sequence.
4-Hydroxy-2-oxoglutarate aldolase, mitochondrial (HOGA1) also known as dihydrodipicolinate synthase-like (DHDPSL) is an enzyme that in humans is encoded by the HOGA1 gene. The protein is one of the enzymes (4-hydroxy-2-oxoglutarate aldolase) involved in metabolism of hydroxyproline to glyoxylate. The enzyme overactivity can form excessive ...
Prolyl 4-hydroxylase subunit alpha-1 is an enzyme that in humans is encoded by the P4HA1 gene. [5] [6] This gene encodes a component of prolyl 4-hydroxylase, a key enzyme in collagen synthesis composed of two identical alpha subunits and two beta subunits. The encoded protein is one of several different types of alpha subunits and provides the ...