1.14.11.29 DALDLEMLAPYISMDDDFQL + 2-oxoglutarate + O2 a HIF-3alpha peptide. Vmax is 120% of the activity with DLDLEMLAPYIPMDDDFQL Homo sapiens ? - ? 404947 1.14.11.29 DALDLEMLAPYISMDDDFQL + 2-oxoglutarate + O2 a HIF-3alpha peptide. Vmax is 120% of the activity with DLDLEMLAPYIPMDDDFQL Homo sapiens DALDLEMLA-((4R)-4-hydroxy-L-proline)-YISMDDDFQL + succinate + CO2 - ? 404948 1.14.11.29 DALDLEMLAPYISMDDDFQL + 2-oxoglutarate + O2 a HIF-3alpha peptide. Vmax is 150% of the activity with DLDLEMLAPYIPMDDDFQL Homo sapiens DALDLEMLA-((4R)-4-hydroxy-L-proline)-YISMDDDFQL + succinate + CO2 - ? 404948 1.14.11.29 DALTLLAPAAGDTIISLDF + 2-oxoglutarate + O2 hybrid substrate derived from C-terminal and N-terminal oxygen-dependent degradation domain Homo sapiens DALTLLA-((4R)-4-hydroxy-L-proline)-AAGDTIISLDF + succinate + CO2 - ? 462416 1.14.11.29 DALTLLAPAAGDTIISLDF + 2-oxoglutarate + O2 substrate derived from N-terminal oxygen-dependent degradation domain Homo sapiens DLDLEMLA-((4R)-4-hydroxy-L-proline)-AAGDTIISLDF + succinate + CO2 - ? 462417 1.14.11.29 DALTLLAPAAGDTIISLFG + 2-oxoglutarate + O2 N-terminal hydroxylation site of HIF-1alpha, Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL Homo sapiens DALTLLA-((4R)-4-hydroxy-L-proline)-AAGDTIISLFG + succinate + CO2 - ? 376646 1.14.11.29 DALTLLAPAAGDTIISLFG + 2-oxoglutarate + O2 N-terminal hydroxylation site of HIF-1alpha, Vmax is 60% of the activity with DLDLEMLAPYIPMDDDFQL Homo sapiens DALTLLA-((4R)-4-hydroxy-L-proline)-AAGDTIISLFG + succinate + CO2 - ? 376646 1.14.11.29 DLDLEALAPYIPADDDFQL + 2-oxoglutarate + O2 - Homo sapiens DLDLEALA-((4R)-4-hydroxy-L-proline)-YIPADDDFQL + succinate + CO2 - ? 441344 1.14.11.29 DLDLEMLAPAIPMDDDFQL + 2-oxoglutarate + O2 Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL Homo sapiens DLDLEMLA-((4R)-4-hydroxy-L-proline)-AIPMDDDFQL + succinate + CO2 - ? 376734 1.14.11.29 DLDLEMLAPGIPMDDDFQL + 2-oxoglutarate + O2 Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL Homo sapiens DLDLEMLA-((4R)-4-hydroxy-L-proline)-GIPMDDDFQL + succinate + CO2 - ? 405032 1.14.11.29 DLDLEMLAPYIPMD + 2-oxoglutarate + O2 Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL Homo sapiens DLDLEMLA-((4R)-4-hydroxy-L-proline)-YIPMD + succinate + CO2 - ? 405033 1.14.11.29 DLDLEMLAPYIPMDD + 2-oxoglutarate + O2 Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL Homo sapiens DLDLEMLA-((4R)-4-hydroxy-L-proline)-YIPMDD + succinate + CO2 - ? 405034 1.14.11.29 DLDLEMLAPYIPMDDDF + 2-oxoglutarate + O2 Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL Homo sapiens DLDLEMLA-((4R)-4-hydroxy-L-proline)-YIPMDDDF + succinate + CO2 - ? 405035 1.14.11.29 DLDLEMLAPYIPMDDDFQL + 2-oxoglutarate + O2 - Homo sapiens DLDLEMLA-((4R)-4-hydroxy-L-proline)-YIPMDDDFQL + succinate + CO2 - ? 405037 1.14.11.29 DLDLEMLAPYIPMDDDFQL + 2-oxoglutarate + O2 peptide derived from HIF-1alpha Homo sapiens DLDLEMLA-((4R)-4-hydroxy-L-proline)-YIPMDDDFQL + succinate + CO2 - ? 405037 1.14.11.29 DLDLEMLAPYIPMDDDFQL + 2-oxoglutarate + O2 substrate derived from C-terminal oxygen-dependent degradation domain Homo sapiens DLDLEMLA-((4R)-4-hydroxy-L-proline)-YIPMDDDFQL + succinate + CO2 - ? 405037 1.14.11.29 DLDLEMLAPYIPMDDDFQL + 2-oxoglutarate + O2 - Homo sapiens ? - ? 441345 1.14.11.29 DLDLEMLAPYIPMDDDFQL + 2-oxoglutarate + O2 - Mus musculus ? - ? 441345 1.14.11.29 DLDLEMLAPYIPMDDDFQLRSFDQ + 2-oxoglutarate + O2 Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL Homo sapiens DLDLEMLA-((4R)-4-hydroxy-L-proline)-YIPMDDDFQLRSFDQ + succinate + CO2 - ? 405038 1.14.11.29 DLDLEMLAPYIPTIISLDF + 2-oxoglutarate + O2 hybrid substrate derived from C-terminal and N-terminal oxygen-dependent degradation domain Homo sapiens DLDLEMLA-((4R)-4-hydroxy-L-proline)-YIPTIISLDF + succinate + CO2 - ? 462458 1.14.11.29 DLEMLAPYIPMDDDFQL + 2-oxoglutarate + O2 Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL Homo sapiens DLEMLA-((4R)-4-hydroxy-L-proline)-YIPMDDDFQL + succinate + CO2 - ? 376742 1.14.11.29 EEPDLSCLAPFVDTYDMMQM + 2-oxoglutarate + O2 hydroxylation site of Caenorhabditis elegans HIF-alpha. Vmax is 60% of the activity with DLDLEMLAPYIPMDDDFQL Homo sapiens ? - ? 405059 1.14.11.29 EEPDLSCLAPFVDTYDMMQM + 2-oxoglutarate + O2 hydroxylation site of Caenorhabditis elegans HIF-alpha. Vmax is 80% of the activity with DLDLEMLAPYIPMDDDFQL Homo sapiens ? - ? 405059 1.14.11.29 ELDLETLAPYIPMDGEDFQ + 2-oxoglutarate + O2 C-terminal hydroxylation site of HIF-2alpha. Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL Homo sapiens ? - ? 405063 1.14.11.29 ELDLETLAPYIPMDGEDFQ + 2-oxoglutarate + O2 C-terminal hydroxylation site of HIF-2alpha. Vmax is 70% of the activity with DLDLEMLAPYIPMDDDFQL Homo sapiens ? - ? 405063 1.14.11.29 ELDLETLAPYIPMDGEDFQ + 2-oxoglutarate + O2 C-terminal hydroxylation site of HIF-2alpha. Vmax is 80% of the activity with DLDLEMLAPYIPMDDDFQL Homo sapiens ELDLETLA-((4R)-4-hydroxy-L-proline)-YIPMDGEDFQ + succinate + CO2 - ? 405064 1.14.11.29 EMLAPYIPMDD + 2-oxoglutarate + O2 Vmax is 30% of the activity with DLDLEMLAPYIPMDDDFQL Homo sapiens EMLA-((4R)-4-hydroxy-L-proline)-YIPMDD + succinate + CO2 - ? 405068 1.14.11.29 EMLAPYIPMDDDFQL + 2-oxoglutarate + O2 Vmax is 100% of the activity with DLDLEMLAPYIPMDDDFQL Homo sapiens EMLA-((4R)-4-hydroxy-L-proline)-YIPMDDDFQL + succinate + CO2 - ? 405069 1.14.11.29 EMLAPYIPMDDDFQL + 2-oxoglutarate + O2 Vmax is 80% of the activity with DLDLEMLAPYIPMDDDFQL Homo sapiens EMLA-((4R)-4-hydroxy-L-proline)-YIPMDDDFQL + succinate + CO2 - ? 405069 1.14.11.29 EPEELAQLAPTPGDAIISLD + 2-oxoglutarate + O2 N-terminal hydroxylation site of HIF-2alpha. Vmax is 30% of the activity with DLDLEMLAPYIPMDDDFQL Homo sapiens ? - ? 405075 1.14.11.29 EPEELAQLAPTPGDAIISLD + 2-oxoglutarate + O2 N-terminal hydroxylation site of HIF-2alpha. Vmax is 70% of the activity with DLDLEMLAPYIPMDDDFQL Homo sapiens ? - ? 405075 1.14.11.29 EPEELAQLAPTPGDAIISLD + 2-oxoglutarate + O2 N-terminal hydroxylation site of HIF-2alpha. Vmax is 80% of the activity with DLDLEMLAPYIPMDDDFQL Homo sapiens ? - ? 405075 1.14.11.29 hypoxia-inducible factor 1 alpha-L-proline + 2-oxoglutarate + O2 - Mus musculus hypoxia-inducible factor 1alpha-trans-4-hydroxy-L-proline + succinate + CO2 - ? 440275 1.14.11.29 hypoxia-inducible factor 1alpha-L-proline + 2-oxoglutarate + O2 - Homo sapiens hypoxia-inducible factor 1alpha-trans-4-hydroxy-L-proline + succinate + CO2 - ? 440276 1.14.11.29 hypoxia-inducible factor HIF1alpha-L-proline + 2-oxoglutarate + O2 - Homo sapiens hypoxia-inducible factor HIF1alpha-trans-4-hydroxy-L-proline + succinate + CO2 - ? 462598 1.14.11.29 hypoxia-inducible factor HIF2alpha-L-proline + 2-oxoglutarate + O2 - Homo sapiens hypoxia-inducible factor HIF2alpha-trans-4-hydroxy-L-proline + succinate + CO2 - ? 462599 1.14.11.29 hypoxia-inducible factor HIF3alpha-L-proline + 2-oxoglutarate + O2 - Homo sapiens hypoxia-inducible factor HIF3alpha-trans-4-hydroxy-L-proline + succinate + CO2 - ? 462600 1.14.11.29 hypoxia-inducible factor-alpha-L-proline + 2-oxoglutarate + O2 - Homo sapiens hypoxia-inducible factor-alpha-trans-4-hydroxy-L-proline + succinate + CO2 - ? 442431 1.14.11.29 hypoxia-inducible factor-alpha-L-proline + 2-oxoglutarate + O2 - Mus musculus hypoxia-inducible factor-alpha-trans-4-hydroxy-L-proline + succinate + CO2 - ? 442431 1.14.11.29 hypoxia-inducible factor-alpha-L-proline + 2-oxoglutarate + O2 - Rattus norvegicus hypoxia-inducible factor-alpha-trans-4-hydroxy-L-proline + succinate + CO2 - ? 442431 1.14.11.29 hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 - Homo sapiens hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2 - ? 402700 1.14.11.29 hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 HIF (hypoxia-inducible factor) is a transcription factor that plays a pivotal role in cellular adaptation to changes in oxygen availability. In the presence of oxygen, HIF is targeted for destruction by an E3 ubiquitin ligase containing the von Hippel-Lindau tumor suppressor protein (pVHL). Human pVHL binds to a short HIF-derived peptide when a conserved proline residue at the core of this peptide is hydroxylated. This protein modifiation may play a key role in mammalian oxygen sensing Homo sapiens hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2 - ? 402700 1.14.11.29 hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 hypoxia-inducible factor (HIF) is a transcriptional complex that plays a central role in the regulation of gene expression by oxygen. In oxygenated and iron replete cells, HIF-alpha subunits are rapidly destroyed by a mechanism that involves ubiquitylation by the von Hippel-Lindau tumor suppressor (pVHL) E3 ligase complex. This process is suppressed by hypoxia and iron chelation, allowing transcriptional activation. The interaction between human pVHL and a specific domain of the HIF-1alpha subunit is regulated through hydroxylation of a proline residue (HIF-1alpha P564) by HIF-alpha prolyl-hydroxylase (HIF-PH). HIF-PH functions directly as a cellular oxygen sensor Homo sapiens hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2 - ? 402700 1.14.11.29 hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 mammalian cells respond to changes in oxygen availability through a conserved pathway that is regulated by the hypoxia-inducible factor (HIF). The alpha subunit of the hypoxia-inducible factor is targeted for degradation under normoxic conditions by a ubiquitin-ligase complex that recognizes a hydroxylated proline residue in hypoxia-inducible factor. HIF prolyl hydroxylase is responsible for this posttranslational modification Homo sapiens hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2 - ? 402700 1.14.11.29 hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 mammalian cells respond to changes in oxygen availability through a conserved pathway that is regulated by the hypoxia-inducible factor (HIF). The alpha subunit of the hypoxia-inducible factor is targeted for degradation under normoxic conditions by a ubiquitin-ligase complex that recognizes a hydroxylated proline residue in hypoxia-inducible factor. HIF prolyl is responsible for this posttranslational modification Homo sapiens hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2 - ? 402700 1.14.11.29 hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 target proline residue: Pro564 in human HIF-alpha. A control peptide in which the target proline residue is replaced by alanine is not modified Homo sapiens hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2 - ? 402700 1.14.11.29 hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 target proline residue: Pro564 in human HIF-alpha. A control peptide in which the target proline residue is replaced by alanine is not modified. The endogenous HIF prolyl hydroxylase, HPH-1 generates by in vitro transcription/translation does not modify peptides containing the L562A, A563G, or Y565A mutations. However, a peptide containing the Pro567 to Gly mutation is an equal, if not better, substrate for the human HPH enzymes Homo sapiens hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2 - ? 402700 1.14.11.29 hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 target proline residue: Pro564 in human HIF-alpha. A control peptide in which the target proline residue is replaced by alanine is not modified. The recombinant HPH-2 purified from Escherichia coli does not modify peptides containing the L562A, A563G, or Y565A mutations. However, a peptide containing the Pro567 to Gly mutation is an equal, if not better, substrate for the human HPH enzymes Homo sapiens hypoxia-inducible factor-(4R)-4-hydroxy-L-proline + succinate + CO2 - ? 402700 1.14.11.29 hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 - Mus musculus hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2 - ? 424834 1.14.11.29 hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 - Homo sapiens hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2 - ? 424834 1.14.11.29 hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 - Mytilus galloprovincialis hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2 - ? 424834 1.14.11.29 hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 - Megalobrama amblycephala hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2 - ? 424834 1.14.11.29 hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 HIF1alpha is a better substrate than HIF2alpha for PHD2 Homo sapiens hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2 - ? 424834 1.14.11.29 hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 PHD enzymes hydroxylates HIF-alpha at prolyl residues present in the transcriptional activation domain N-TAD Homo sapiens hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2 - ? 424834 1.14.11.29 hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 PHD2 hydroxylates Pro402 and/or Pro564 of HIF-1alpha Homo sapiens hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2 - ? 424834 1.14.11.29 hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 differential regulation of HIF1alpha and HIF2alpha at the N-terminal oxygen-dependent degradation domain site by PHD2 Homo sapiens hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2 - ? 424834 1.14.11.29 hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 hydroxylation at P402 and P564 Homo sapiens hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2 - ? 424834 1.14.11.29 hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 hydroxylation of the proline residue in the HIF-1alpha (556-574) peptide substrate, sequence of residues 556-574: DLDLEMLAPYIPMDDDFQL Homo sapiens hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2 - ? 424834 1.14.11.29 hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 the HIF1alpha C-terminal oxygen-dependent degradation domain is highly preferred for hydroxylation, no N-terminal oxygen-dependent degradation domain hydroxylation for both HIF2alpha and HIF1alpha Homo sapiens hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2 - ? 424834 1.14.11.29 hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 the PHD1 reaction at the N-terminal oxygen-dependent degradation domain site shows low level hydroxylation Homo sapiens hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2 - ? 424834 1.14.11.29 hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 hypoxia-inducible factor 1alpha is hydroxylated at Pro402 and Pro564 Drosophila melanogaster hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2 - ? 424834 1.14.11.29 hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 hypoxia-inducible factor 1alpha is hydroxylated at Pro402 and Pro564 Caenorhabditis elegans hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2 - ? 424834 1.14.11.29 hypoxia-inducible factor-L-proline peptide + 2-oxoglutarate + O2 peptide substrate is a peptide derived from the natural sequence of HIF-1alpha residues 556-574 Homo sapiens hypoxia-inducible factor-trans-4-hydroxy-L-proline peptide + succinate + CO2 hydroxylation at Pro564 ? 426496 1.14.11.29 hypoxia-inducible factor-proline + 2-oxoglutarate + O2 HIF-1alpha Homo sapiens hypoxia-inducible factor-(3S)-3-hydroxy-proline + succinate + CO2 - ? 424835 1.14.11.29 hypoxia-inducible factor1alpha C-terminal oxygen-dependent degradation domain-L-proline + 2-oxoglutarate + O2 - Homo sapiens hypoxia-inducible factor1alpha C-terminal oxygen-dependent degradation domain-trans-4-hydroxy-L-proline + succinate + CO2 - ? 426498 1.14.11.29 hypoxia-inducible factor1alpha C-terminal oxygen-dependent degradation domain-L-proline + 2-oxoglutarate + O2 low activity Homo sapiens hypoxia-inducible factor1alpha C-terminal oxygen-dependent degradation domain-trans-4-hydroxy-L-proline + succinate + CO2 - ? 426498 1.14.11.29 hypoxia-inducible factor1alpha N-terminal oxygen-dependent degradation domain-L-proline + 2-oxoglutarate + O2 - Homo sapiens hypoxia-inducible factor1alpha N-terminal oxygen-dependent degradation domain-trans-4-hydroxy-L-proline + succinate + CO2 - ? 426500 1.14.11.29 hypoxia-inducible factor1alpha N-terminal oxygen-dependent degradation domain-L-proline + 2-oxoglutarate + O2 low activity Homo sapiens hypoxia-inducible factor1alpha N-terminal oxygen-dependent degradation domain-trans-4-hydroxy-L-proline + succinate + CO2 - ? 426500 1.14.11.29 hypoxia-inducible factor2alpha C-terminal oxygen dependent degradation domain-L-proline + 2-oxoglutarate + O2 - Homo sapiens hypoxia-inducible factor2alpha C-terminal oxygen dependent degradation domain-trans-4-hydroxy-L-proline + succinate + CO2 - ? 426501 1.14.11.29 hypoxia-inducible factor2alpha C-terminal oxygen-dependent degradation domain-L-proline + 2-oxoglutarate + O2 - Homo sapiens hypoxia-inducible factor2alpha C-terminal oxygen-dependent degradation domain-trans-4-hydroxy-L-proline + succinate + CO2 - ? 426502 1.14.11.29 hypoxia-inducible factor2alpha N-terminal oxygen dependent degradation domain-L-proline + 2-oxoglutarate + O2 - Homo sapiens hypoxia-inducible factor2alpha N-terminal oxygen dependent degradation domain-trans-4-hydroxy-L-proline + succinate + CO2 - ? 426503 1.14.11.29 L-ascorbate + 2-oxoglutarate + O2 L-ascorbate is a co-substrate of HIF prolyl hydroxylase PHD that may compete for the binding site of 2-oxoglutarate in the enzyme active center Homo sapiens ? + succinate + CO2 - ? 462637 1.14.11.29 LAPYIPMDDDFQL + 2-oxoglutarate + O2 Vmax is 90% of the activity with DLDLEMLAPYIPMDDDFQL Homo sapiens LA-((4R)-4-hydroxy-L-proline)-YIPMDDDFQL + succinate + CO2 - ? 405704 1.14.11.29 additional information the enzyme requires long peptide substrates. No hydroxylation of: Leu-Ala-Pro, Leu-Ala-Pro-Tyr, Leu-Glu-Met-Leu-Ala-Pro, and Leu-Glu-Met-Leu-Ala-Pro-Tyr Homo sapiens ? - ? 89 1.14.11.29 additional information HIF prolyl-4-hydroxylase 2 substrate binding analysis using isolated sequences of the C-terminal oxygen degradation domain DLDLEALAP564YIPADDDFQL mutant M561A/M568A, and the N-terminal oxygen degradation domain DALTLLAP402AAGDTIISLDYG mutant F413Y, overview Homo sapiens ? - ? 89 1.14.11.29 additional information substrate selectivity of PHD2 by kinetic competition assays, varied ionic strength, and global protein flexibility using amide H/D exchange, overview Homo sapiens ? - ? 89 1.14.11.29 additional information the substrate contains a C-terminal and a N-terminal oxygen-dependent degradation domain, as well as a C-terminal transactivation domain Homo sapiens ? - ? 89 1.14.11.29 additional information the subtrate contains a C-terminal and a N-terminal oxygen-dependent degradation domain, as well as a C-terminal transactivation domain Homo sapiens ? - ? 89 1.14.11.29 additional information isozyme PHD2 is more active on hypoxia-inducible factor-1alpha than on hypoxia-inducible factor-2alpha, whereas PHD1 and PHD3 hydroxylate hypoxia-inducible factor-2alpha more efficiently Homo sapiens ? - ? 89 1.14.11.29 additional information prolyl hydroxylation is not assigned on any of the teste non-HIF substrate sites. Recombinant PHD enzymes provide no support for the wide range of non-HIF PHD substrates reported Homo sapiens ? - - 89