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1.14.11.29: hypoxia-inducible factor-proline dioxygenase

This is an abbreviated version!
For detailed information about hypoxia-inducible factor-proline dioxygenase, go to the full flat file.

Word Map on EC 1.14.11.29

Reaction

hypoxia-inducible factor-L-proline
+
2-oxoglutarate
 +
O2
=
hypoxia-inducible factor-(4R)-4-hydroxy-L-proline
 +
succinate
 +
CO2

Synonyms

Egl nine homolog 1, EGLN, EGLN1, Egln2, EGLN3, factor inhibiting HIF, FIH, HIF hydroxylase, HIF prolyl, HIF prolyl 4-hydroxylase, HIF prolyl hydroxylase, HIF-1alpha PHD3, HIF-1alpha prolyl hydroxylase 3, HIF-alpha prolyl-hydroxylase, HIF-P4H-1, HIF-P4H-2, HIF-P4H-3, HIF-PH, Hif-prolyl hydroxylase, HIF-prolyl hydroxylase domain 2, HIF-prolyl hydroxylase-2, HPH-1, HPH-2, HPH-3, hydroxylase domain enzyme, hypoxia-inducible factor prolyl hydroxylase 2, hypoxia-inducible factor prolyl hydroxylase domain 2, P4H-TM, PHD, PHD1, PHD2, PHD3, proline hydroxylase domain 2, prolyl 4-hydroxylase, prolyl hydroxylase, prolyl hydroxylase domain, prolyl hydroxylase domain protein, prolyl hydroxylase domain protein 2, prolyl hydroxylase-2, prolyl-4-hydroxylase 2, prolyl-4-hydroxylase domain 2, transmembrane prolyl 4-hydroxylase

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
                1.14.11.29 hypoxia-inducible factor-proline dioxygenase

Engineering

Engineering on EC 1.14.11.29 - hypoxia-inducible factor-proline dioxygenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D137A
mutation eliminates prolyl hydroxylase activity of HPH-1
D315E
substitution of the Fe(II)-binding aspartate for a glutamate residue manifests significantly reduced Fe(II) binding, yet maintains catalytic activity with a 5fold faster reaction with O2
H135A
mutation eliminates prolyl hydroxylase activity of HPH-1
H196A
mutation eliminates prolyl hydroxylase activity of HPH-1
R367K
inactive mutant of HIF-P4H-1
R383K
disruption of 2OG binding in this variant does not accelerate O2 activation
T387A
the mutant shows 15fold increased turnover at limiting O2 concentrations compared to the wild type enzyme
T387N
the mutant shows about 2fold reduced turnover at limiting O2 concentrations compared to the wild type enzyme
additional information