| D007700 |
Kinetics |
The rate dynamics in chemical or physical systems. |
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| D008240 |
Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase |
A mixed-function oxygenase that catalyzes the hydroxylation of peptidyllysine, usually in protocollagen, to peptidylhydroxylysine. The enzyme utilizes molecular oxygen with concomitant oxidative decarboxylation of the cosubstrate 2-oxoglutarate to succinate. EC 1.14.11.4. |
Lysine 2-Oxoglutarate Dioxygenase,Lysine Hydroxylase,Protocollagen Lysyl Hydroxylase,Collagen Lysyl Hydroxylase,Lysyl Hydroxylase,2-Oxoglutarate 5-Dioxygenase Procollagen-Lysine,2-Oxoglutarate Dioxygenase, Lysine,5-Dioxygenase Procollagen-Lysine, 2-Oxoglutarate,Dioxygenase, Lysine 2-Oxoglutarate,Hydroxylase, Collagen Lysyl,Hydroxylase, Lysine,Hydroxylase, Lysyl,Hydroxylase, Protocollagen Lysyl,Lysine 2 Oxoglutarate Dioxygenase,Procollagen Lysine, 2 Oxoglutarate 5 Dioxygenase |
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| D011393 |
Procollagen-Proline Dioxygenase |
A mixed-function oxygenase that catalyzes the hydroxylation of a prolyl-glycyl containing peptide, usually in PROTOCOLLAGEN, to a hydroxyprolylglycyl-containing-peptide. The enzyme utilizes molecular OXYGEN with a concomitant oxidative decarboxylation of 2-oxoglutarate to SUCCINATE. The enzyme occurs as a tetramer of two alpha and two beta subunits. The beta subunit of procollagen-proline dioxygenase is identical to the enzyme PROTEIN DISULFIDE-ISOMERASES. |
Protocollagen Prolyl Hydroxylase,Procollagen Prolyl 4-Hydroxylase,4-Hydroxylase, Procollagen Prolyl,Dioxygenase, Procollagen-Proline,Hydroxylase, Protocollagen Prolyl,Procollagen Proline Dioxygenase,Procollagen Prolyl 4 Hydroxylase,Prolyl 4-Hydroxylase, Procollagen,Prolyl Hydroxylase, Protocollagen |
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| D002478 |
Cells, Cultured |
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others. |
Cultured Cells,Cell, Cultured,Cultured Cell |
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| D003094 |
Collagen |
A polypeptide substance comprising about one third of the total protein in mammalian organisms. It is the main constituent of SKIN; CONNECTIVE TISSUE; and the organic substance of bones (BONE AND BONES) and teeth (TOOTH). |
Avicon,Avitene,Collagen Felt,Collagen Fleece,Collagenfleece,Collastat,Dermodress,Microfibril Collagen Hemostat,Pangen,Zyderm,alpha-Collagen,Collagen Hemostat, Microfibril,alpha Collagen |
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| D005347 |
Fibroblasts |
Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules. |
Fibroblast |
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| D006801 |
Humans |
Members of the species Homo sapiens. |
Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man |
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| D006901 |
Hydroxylysine |
A hydroxylated derivative of the amino acid LYSINE that is present in certain collagens. |
(2S,5R)-2,6-Diamino-5-hydroxyhexanoic Acid,2,6-Diamino-5-hydroxyhexanoic Acid,5-Hydroxylysine,Lysine, 5-Hydroxy-,2,6 Diamino 5 hydroxyhexanoic Acid,5 Hydroxylysine,Lysine, 5 Hydroxy |
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| D006909 |
Hydroxyproline |
A hydroxylated form of the imino acid proline. A deficiency in ASCORBIC ACID can result in impaired hydroxyproline formation. |
Oxyproline,4-Hydroxyproline,cis-4-Hydroxyproline,4 Hydroxyproline,cis 4 Hydroxyproline |
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| D001205 |
Ascorbic Acid |
A six carbon compound related to glucose. It is found naturally in citrus fruits and many vegetables. Ascorbic acid is an essential nutrient in human diets, and necessary to maintain connective tissue and bone. Its biologically active form, vitamin C, functions as a reducing agent and coenzyme in several metabolic pathways. Vitamin C is considered an antioxidant. |
Vitamin C,Ascorbic Acid, Monosodium Salt,Ferrous Ascorbate,Hybrin,L-Ascorbic Acid,Magnesium Ascorbate,Magnesium Ascorbicum,Magnesium di-L-Ascorbate,Magnorbin,Sodium Ascorbate,Acid, Ascorbic,Acid, L-Ascorbic,Ascorbate, Ferrous,Ascorbate, Magnesium,Ascorbate, Sodium,L Ascorbic Acid,Magnesium di L Ascorbate,di-L-Ascorbate, Magnesium |
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