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Literature summary extracted from

  • Myllykoski, M.; Sutinen, A.; Koski, M.; Kallio, J.; Raasakka, A.; Myllyharju, J.; Wierenga, R.; Koivunen, P.
    Structure of transmembrane prolyl 4-hydroxylase reveals unique organization of EF and dioxygenase domains (2021), J. Biol. Chem., 296, 100197 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.11.29 expression in Escherichia coli Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.11.29 sitting-drop vapor-diffusion method, the crystal structure reveals an EF domain with two Ca2+-binding motifs inserted within the catalytic domain. A substrate-binding groove is formed between the EF domain and the conserved core of the catalytic domain Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.11.29 endoplasmic reticulum the enzyme is composed of an N-terminal cytoplasmic tail, a membrane-anchoring transmembrane helix, and a unique combination of a Ca2+-binding EF domain and a catalytic domain that is located within the ER lumen membrane Homo sapiens 5783
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Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.11.29 Ca2+ the crystal structure reveals an EF domain with two Ca2+-binding motifs inserted within the catalytic domain. The proximity of the EF domain to the active site suggests that Ca2+ binding is relevant to the catalytic activity. Functional analysis demonstrates that Ca2+-binding affinity of P4H-TM is within the range of physiological Ca2+ concentration in the endoplasmic reticulum. P4H-TM is found both as a monomer and a dimer in the solution, but the monomer-dimer equilibrium is not regulated by Ca2+ Homo sapiens
1.14.11.29 Fe2+ the catalytic site contained bound Fe2+ and N-oxalylglycine Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.14.11.29 Homo sapiens Q9NXG6
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.11.29
-
 Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
1.14.11.29 P4H-TM
-
 Homo sapiens
1.14.11.29 transmembrane prolyl 4-hydroxylase
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 Homo sapiens

General Information

EC Number General Information Comment Organism
1.14.11.29 physiological function prolyl 4-hydroxylases (P4Hs) catalyze post-translational hydroxylation of peptidyl proline residues Homo sapiens