User:Cboursnell/Sandbox/2OG-FeII Oxy
< User:Cboursnell | Sandbox
| 2OG-FeII_Oxy | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 the structure of acc oxidase | |||||||||
| Identifiers | |||||||||
| Symbol | 2OG-FeII_Oxy | ||||||||
| Pfam | PF03171 | ||||||||
| Pfam clan | CL0029 | ||||||||
| InterPro | IPR005123 | ||||||||
| PROSITE | PDOC00165 | ||||||||
| SCOP2 | 1ips / SCOPe / SUPFAM | ||||||||
| |||||||||
This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily.[1] This family includes the C-terminal of prolyl 4-hydroxylase alpha subunit. The holoenzyme has the activity (EC) catalysing the reaction:
Procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2
The full enzyme consists of a alpha2 beta2 complex with the alpha subunit contributing most of the parts of the active site.[2] The family also includes lysyl hydrolases, isopenicillin synthases and AlkB.
References[edit]
- ^ Aravind L, Koonin EV (2001). "The DNA-repair protein AlkB, EGL-9, and leprecan define new families of 2-oxoglutarate- and iron-dependent dioxygenases". Genome Biol. 2 (3): RESEARCH0007. doi:10.1186/gb-2001-2-3-research0007. PMC 30706. PMID 11276424.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ Helaakoski T, Annunen P, Vuori K, MacNeil IA, Pihlajaniemi T, Kivirikko KI (May 1995). "Cloning, baculovirus expression, and characterization of a second mouse prolyl 4-hydroxylase alpha-subunit isoform: formation of an alpha 2 beta 2 tetramer with the protein disulfide-isomerase/beta subunit". Proc. Natl. Acad. Sci. U.S.A. 92 (10): 4427–4431. doi:10.1073/pnas.92.10.4427. PMC 41957. PMID 7753822.
{{cite journal}}: CS1 maint: date and year (link) CS1 maint: multiple names: authors list (link)