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(2S,4S)-4-fluoroproline + 2-oxoglutarate + O2
(2S)-4-oxoproline + fluoride
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development and evaluation of an assay method that continuously and directly detects turnover of the proline-containing substrate. The assay is based on (2S,4S)-4-fluoroproline, a proline analogue that is transformed into (2S)-4-oxoproline and inorganic fluoride by P4H using a fluoride ion-selective electrode for detection
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(Ala-Pro-Gly)5 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
recombinant enzyme
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(Ala-Thr-Pro-Pro-Pro-Val)3 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
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(ATPPPV)3 + 2-oxoglutarate + O2
trans-4-hydroxy-L-proline (ATPPPV)3 + succinate + CO2
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(Gly-Ala-Pro)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
(Gly-Pro-4Hyp)5 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
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?
(Gly-Pro-Ala)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
(Gly-Pro-Pro)10 + 2-oxoglutarate + O2
?
(GPP)10 + 2-oxoglutarate + O2
?
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(L-Pro-L-Ala-L-Pro-L-Lys)2 + 2-oxoglutarate + O2
(L-Pro-L-Ala-L-Pro-L-Lys)2-trans-4-hydroxy-L-proline + succinate + CO2
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r
(L-Pro-L-Ala-L-Pro-L-Lys)3 + 2-oxoglutarate + O2
(L-Pro-L-Ala-L-Pro-L-Lys)3-trans-4-hydroxy-L-proline + succinate + CO2
(L-Pro-L-Glu-L-Pro-L-Pro-L-Ala)5 L-proline + 2-oxoglutarate + O2
(L-Pro-L-Glu-L-Pro-L-Pro-L-Ala)5 trans-4-hydroxy-L-proline + succinate + CO2
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(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
(L-Pro-L-Pro-Gly)10 L-proline + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10 trans-4-hydroxy-L-proline + succinate + CO2
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44.8% of the activity with (L-Pro-L-Glu-L-Pro-L-Pro-L-Ala)5 L-proline
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(L-Pro-L-Pro-Gly)2 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)2-trans-4-hydroxy-L-proline + succinate + CO2
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r
(L-Pro-L-Pro-Gly)5 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)5-trans-4-hydroxy-L-proline + succinate + CO2
(L-prolylglycyl-L-prolyl)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide
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molecular weight of the peptide substrate: about 4000
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?
(L-Ser-L-Pro)19 L-proline + 2-oxoglutarate + O2
(L-Ser-L-Pro)19 trans-4-hydroxy-L-proline + succinate + CO2
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(L-Ser-L-Pro-L-Ala-L-Pro-L-Pro)5 L-proline + 2-oxoglutarate + O2
(L-Ser-L-Pro-L-Ala-L-Pro-L-Pro)5 trans-4-hydroxy-L-proline + succinate + CO2
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(L-Ser-L-Pro-L-Glu-L-Pro-L-Pro)5 L-proline + 2-oxoglutarate + O2
(L-Ser-L-Pro-L-Glu-L-Pro-L-Pro)5 trans-4-hydroxy-L-proline + succinate + CO2
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(L-Ser-L-Pro-L-Lys-L-Pro-L-Pro)5 L-proline + 2-oxoglutarate + O2
(L-Ser-L-Pro-L-Lys-L-Pro-L-Pro)5 trans-4-hydroxy-L-proline + succinate + CO2
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(Pro-Ala-Gly)5 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
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(Pro-Ala-Pro-Lys)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
(Pro-Glu-Pro-Pro-Ala)5 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
(Pro-Gly-Pro)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
(Pro-Pro-Gly)10 + 2-oxoglutarate + O2
? + succinate + CO2
(Pro-Pro-Gly)10 + 2-oxoglutarate + O2
trans-4-hydroxy-L-proline (Pro-Pro-Gly)10 + succinate + CO2
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(Pro-Pro-Gly)10 + O2
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(Pro-Pro-Gly)10 L-proline + 2-oxoglutarate + O2
(Pro-Pro-Gly)10 trans-4-hydroxy-L-proline + succinate + CO2
(Pro-Pro-Gly)2 L-proline + 2-oxoglutarate + O2
(Pro-Pro-Gly)2 trans-4-hydroxy-L-proline + succinate + CO2
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
(Ser-Pro)5 + O2
?
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the (Ser-Pro)5 peptide is found only in molecules A and C of the four polypeptides forming the enzyme
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(Ser-Pro-Lys-Pro-Pro)5 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
100-amino acid alpha1(I) collagen fragment + 2-oxoglutarate + O2
?
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r
100-amino acid alpha1(I) collagen fragment L-proline + 2-oxoglutarate + O2
100-amino acid alpha1(I) collagen fragment trans-4-hydroxy-L-proline + succinate + CO2
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2-oxoglutarate + O2 + ascorbate
succinate + dehydroascorbate + CO2 + H2O
510-amino acid alpha1(I) collagen fragment + 2-oxoglutarate + O2
?
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r
510-amino acid alpha1(I) collagen fragment L-proline + 2-oxoglutarate + O2
510-amino acid alpha1(I) collagen fragment trans-4-hydroxy-L-proline + succinate + CO2
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Arg-Gly-(Pro-Pro-Gly)5 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
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Argonaute 2 + 2-oxoglutarate + O2
4-hydroxyproline-Argonaute 2 + succinate + CO2
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regulation of Ago 2 protein activity via substrate protein stability involving Ago Pro700 residue, the Ago protein mutant P700A is destabilized, overview
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Argonaute protein + 2-oxoglutarate + O2
4-hydroxyproline-Argonaute protein + succinate + CO2
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i.e. GERp95 or Golgi endoplasmic reticulum protein 95 kDa. Recombinant substrate proteins expressed in HeLa S3 cells. Ago2 is a cytoplasmically exposed, peripheral membrane protein that exists in a protease-resistant complex. Hydroxylation of Pro700, which is important for Ago2 stability, but not of Ago1 or Ago3 stability, identification by mass spectrometric analysis. In vitro, both Ago2 and Ago4 seem to be more efficiently hydroxylated than Ago1 and Ago3 by recombinant human isozyme C-P4H(I)
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Asp-Ala-Leu-Thr-Leu-Leu-Ala-Pro-Ala-Ala-Gly-Asp-Thr-Ile-Ile-Ser-Leu-Phe-Gly + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
peptide representing hypoxia-inducible transcription factor alpha sequences
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Asp-Leu-Asp-Leu-Glu-Met-Leu-Ala-Pro-Tyr-Ile-Pro-Met-Asp-Asp-Asp-Phe-Gln-Leu + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
peptide representing hypoxia-inducible transcription factor alpha sequences
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biotin-Ahx-DLDLEALAP564YIPADDDFQL + 2-oxoglutarate + O2
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19mer HIF peptide not containing cysteine is used, in order to rule out an involvement of the cysteine nitrosylation
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bradykinin + 2-oxoglutarate + O2
4-hydroxyproline containing bradykinin
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carboxymethylated collagen L-proline + 2-oxoglutarate + O2
carboxymethylated collagen-trans-4-hydroxy-L-proline + succinate + CO2
collagen + 2-oxoglutarate + O2
4-hydroxyproline containing collagen + succinate + CO2
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DALTLLAPAAGDTIISLDYG + 2-oxoglutarate + O2
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NODD peptide derived from native HIF-1alpha395-414
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DALTLLAPAAGDTIISLFG + 2-oxoglutarate + O2
DALTLLA-((4R)-4-hydroxy-L-proline)-AAGDTIISLFG + succinate + CO2
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dansyl-Gly-Phe-Pro-Gly-OEt + 2-oxoglutarate + O2
dansyl-Gly-Phe-4-hydroxy-L-Pro-Gly-OEt + succinate + CO2
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dansyl-Gly-Phe-Pro-Gly-OEt + 2-oxoglutarate + O2
dansyl-Gly-Phe-trans-4-hydroxy-L-proline-Gly-OEt + succinate + CO2
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DLDLEALAPYIPADDDFQL + 2-oxoglutarate + O2
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CODD peptide derived from native HIF-1alpha556-574. PHD2 preferred CODD by 20fold over NODD
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DLDLEMLAPAIPMDDDFQL + 2-oxoglutarate + O2
DLDLEMLA-((4R)-4-hydroxy-L-proline)-AIPMDDDFQL + succinate + CO2
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DLDLEMLAPAIPMDDDFQLRSFDQ + 2-oxoglutarate + O2
DLDLEMLAPAIPMDDDFQLRSFDQ trans-4-hydroxy-L-proline + succinate + CO2
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DLDLEMLAPGIPMDDDFQL + 2-oxoglutarate + O2
DLDLEMLAPGIPMDDDFQL trans-4-hydroxy-L-proline + succinate + CO2
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DLDLEMLAPYIPMD + 2-oxoglutarate + O2
DLDLEMLAPYIPMD trans-4-hydroxy-L-proline + succinate + CO2
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DLDLEMLAPYIPMDD + 2-oxoglutarate + O2
DLDLEMLAPYIPMDD trans-4-hydroxy-L-proline + succinate + CO2
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DLDLEMLAPYIPMDDDF + 2-oxoglutarate + O2
DLDLEMLAPYIPMDDDF trans-4-hydroxy-L-proline + succinate + CO2
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DLDLEMLAPYIPMDDDFQL + 2-oxoglutarate + O2
DLDLEMLAPYIPMDDDFQL trans-4-hydroxy-L-proline + succinate + CO2
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DLDLEMLAPYIPMDDDFQLRSFDQ + 2-oxoglutarate + O2
DLDLEMLAPYIPMDDDFQLRSFDQ trans-4-hydroxy-L-proline + succinate + CO2
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DLEMLAPYIPMDDDFQL + 2-oxoglutarate + O2
DLEMLA-((4R)-4-hydroxy-L-proline)-YIPMDDDFQL + succinate + CO2
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EMLAPYIPMDDDFQL + 2-oxoglutarate + O2
EMLAPYIPMDDDFQL trans-4-hydroxy-L-proline + succinate + CO2
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Glu-Gly-(Pro-Pro-Gly)5 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
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Gly-Pro8 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide
Gly-Val-Pro-Gly-Val + 2-oxoglutarate + O2
Gly-Val-4-hydroxyproline-Gly-Val + succinate + CO2
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?
human procollagen-like (P-P-G)10 peptide L-proline + 2-oxoglutarate + O2
human procollagen-like (P-P-G)10 peptide trans-4-hydroxy-L-proline + succinate + CO2
Q81LZ8
4 different peptide sequences, anaerobic conditions
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human procollagen-like (P-P-G)5 peptide L-proline + 2-oxoglutarate + O2
human procollagen-like (P-P-G)5 peptide trans-4-hydroxy-L-proline + succinate + CO2
Q81LZ8
5 different peptide sequences, anaerobic conditions
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hypoxia-induced factor alpha oxygen-dependent degradation domain L-proline + 2-oxoglutarate + O2
hypoxia-induced factor alpha oxygen-dependent degradation domain L-4-hydroxyproline + succinate + CO2
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in vitro hydroxylation of two proline residues, with preference for C-terminal proline
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hypoxia-inducible factor alpha L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor alpha trans-4-hydroxy-L-proline + succinate + CO2
hypoxia-inducible factor L-proline + 2-oxoglutarate + O2
hypoxia inducible factor trans-4-hydroxy-L-proline + succinate + CO2
hypoxia-inducible factor L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor trans-4-hydroxy-L-proline + succinate + CO2
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hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
L-Ala-(L-Pro)4-Gly-L-Ile-L-Pro-Gly-L-Tyr-(L-Pro)2-L-Ala-(L-Pro)4-Gly-L-Val-Gly-(L-Pro)4-L-Gln-Gly L-proline + 2-oxoglutarate + O2
L-Ala-(L-Pro)4-Gly-L-Ile-L-Pro-Gly-L-Tyr-(L-Pro)2-L-Ala-(L-Pro)4-Gly-L-Val-Gly-(L-Pro)4-L-Gln-Gly trans-4-hydroxy-L-proline + succinate + CO2
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peptide substrate representing proline-rich proteins expressed in the pharyngeal gland cells. 380% of the activity with (L-Pro-L-Glu-L-Pro-L-Pro-L-Ala)5 L-proline
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L-Pro-L-Ala-L-Pro-L-Lys + 2-oxoglutarate + O2
L-Pro-L-Ala-L-Pro-L-Lys-trans-4-hydroxy-L-proline + succinate + CO2
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r
L-Pro-L-Ile-(L-Pro)7-L-Leu-L-Pro-L-Gln-L-Asn-L-Leu-L-Ser-Gly-L-Ala-L-Pro L-proline + 2-oxoglutarate + O2
L-Pro-L-Ile-(L-Pro)7-L-Leu-L-Pro-L-Gln-L-Asn-L-Leu-L-Ser-Gly-L-Ala-L-Pro trans-4-hydroxy-L-proline + succinate + CO2
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peptide substrate representing proline-rich proteins expressed in the pharyngeal gland cells. 610% of the activity with (L-Pro-L-Glu-L-Pro-L-Pro-L-Ala)5 L-proline
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L-Pro-L-Pro-Gly + 2-oxoglutarate + O2
L-Pro-L-Pro-Gly-trans-4-hydroxy-L-proline + succinate + CO2
L-proline + 2-oxoglutarate + O2
4-hydroxyproline + succinate + CO2
LAPYIPMDDDFQL + 2-oxoglutarate + O2
LAPYIPMDDDFQL trans-4-hydroxy-L-proline + succinate + CO2
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Lys-Pro-Ala + 2-oxoglutarate + O2
Lys-4-hydroxyproline-Ala + succinate + CO2
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recombinant enzyme
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lysine hydroxylated protocollagen + 2-oxoglutarate + O2
lysine 4-hydroxyproline containing protocollagen + succinate + CO2
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octa-L-proline + 2-oxoglutarate + O2
4-hydroxyproline containing peptide
PEG-Gly-Tyr-4-fluoroproline-GlyOEt + 2-oxoglutarate + O2
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peptidyl L-proline + 2-oxoglutarate + O2
peptidyl-trans-4-hydroxy-L-proline + succinate + CO2
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r
poly L-proline + 2-oxoglutarate + O2
poly trans-4-hydroxy-L-proline + succinate + CO2
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molecular weights of 5000 Da, 8000 Da and 32000 Da, respectively
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poly(ethylene glycol)-Gly-L-Tyr-(2S)-4-thiaproline-Gly-OCH2CH2OH + 2-oxoglutarate + O2
poly(ethylene glycol)-Gly-L-Tyr-L-(2S,4R)-thiaoxoproline-Gly-OCH2CH2OH + ? + CO2
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6% of the activity with L-prolyl peptide substrate
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poly(ethylene glycol)-Gly-L-Tyr-L-(2S,4S)-4-fluoroproline-Gly-OCH2CH2OH + 2-oxoglutarate + O2
poly(ethylene glycol)-Gly-L-Tyr-L-(2S)-4-oxoproline-Gly-OCH2CH2OH + ? + CO2
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26% of the activity with L-prolyl peptide substrate
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poly(ethylene glycol)-Gly-L-Tyr-L-Pro-Gly-OCH2CH2OH + 2-oxoglutarate + O2
poly(ethylene glycol)-Gly-L-Tyr-L-(2S,4R)-4-hydroxy-Pro-Gly-OCH2CH2OH + succinate + CO2
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poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
poly(L-Pro) + 2-oxoglutarate + O2
poly(trans-4-hydroxy-L-proline) + succinate + CO2
poly(L-proline) + 2-oxoglutarate + O2
poly trans-4-hydroxy-L-proline + succinate + CO2
Paramecium bursaria Chlorella virus-1
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poly(L-proline) + 2-oxoglutarate + O2
poly(trans-4-hydroxy-L-proline) + succinate + CO2
poly(L-proline) + O2
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substrate MW is 5000 kDa
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procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-(2S,4R)-4-hydroxy-L-proline + succinate + CO2
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
protocollagen type I L-proline + 2-oxoglutarate + O2
protocollagen type I-trans-4-hydroxy-L-proline + succinate + CO2
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r
protocollagen type I L-proline+ 2-oxoglutarate + O2
protocollagen type I-trans-4-hydroxy-L-proline + succinate + CO2
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r
Ser-Pro-Pro-Pro-Pro-Val-Ser-Pro-Pro-Pro-Val-Ser-Pro-Pro-Pro-Pro-Val + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
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Ser-Pro-Pro-Pro-Val-Tyr-Lys-Ser-Pro-Pro-Pro-Pro-Val-Lys-His-Tyr-Ser-Pro-Pro-Pro-Val + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
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SPPPPVSPPPVSPPPPV + 2-oxoglutarate + O2
trans-4-hydroxy-L-proline SPPPPVSPPPVSPPPPV + succinate + CO2
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SPPPPVYKSPPPPVKHYSPPPV + 2-oxoglutarate + O2
trans-4-hydroxy-L-proline SPPPPVYKSPPPPVKHYSPPPV + succinate + CO2
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tert-butyloxycarbonyl-Gly-Val-Pro-Gly-Val-OH + 2-oxoglutarate + O2
tert-butyloxycarbonyl-Gly-Val-Hyp-Gly-Val-OH + succinate + CO2
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tert-butyloxycarbonyl-L-Pro-L-Pro-Gly + 2-oxoglutarate + O2
tert-butyloxycarbonyl-L-Pro-L-Pro-Gly-trans-4-hydroxy-L-proline + succinate + CO2
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r
tert-butyloxycarbonyl-Pro-Pro-Ala-Pro-OH + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
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tert-butyloxycarbonyl-Pro-Pro-Gln-Pro-OCH3 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
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tert-butyloxycarbonyl-Pro-Pro-Gly-Pro + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
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tert-butyloxycarbonyl-Pro-Pro-Gly-Pro-NHCH3 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
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tert-butyloxycarbonyl-Pro-Pro-Gly-Pro-Pro-OH + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
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tert-butyloxycarbonyl-Pro8 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide
tert-butyloxycarbonyl-Val-Pro-Gly-Val-OH + 2-oxoglutarate + O2
tert-butyloxycarbonyl-Val-Hyp-Gly-Val-OH + succinate + CO2
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additional information
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(Gly-Ala-Pro)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
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less than 10% relative activity with respect to (Gly-Pro-Ala)n
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(Gly-Ala-Pro)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
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active substrate
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(Gly-Pro-Ala)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
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the best substrate
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(Gly-Pro-Ala)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
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poor substrate
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(Gly-Pro-Pro)10 + 2-oxoglutarate + O2
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(Gly-Pro-Pro)10 + 2-oxoglutarate + O2
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Q81LZ8
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(L-Pro-L-Ala-L-Pro-L-Lys)3 + 2-oxoglutarate + O2
(L-Pro-L-Ala-L-Pro-L-Lys)3-trans-4-hydroxy-L-proline + succinate + CO2
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r
(L-Pro-L-Ala-L-Pro-L-Lys)3 + 2-oxoglutarate + O2
(L-Pro-L-Ala-L-Pro-L-Lys)3-trans-4-hydroxy-L-proline + succinate + CO2
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r
(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
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r
(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
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r
(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
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r
(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
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r
(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
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r
(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
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r
(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
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r
(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
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r
(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
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r
(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
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r
(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
Paramecium bursaria Chlorella virus-1
-
-
-
-
r
(L-Pro-L-Pro-Gly)10 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)10-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
(L-Pro-L-Pro-Gly)5 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)5-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
r
(L-Pro-L-Pro-Gly)5 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)5-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
(L-Pro-L-Pro-Gly)5 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)5-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
(L-Pro-L-Pro-Gly)5 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)5-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
(L-Pro-L-Pro-Gly)5 + 2-oxoglutarate + O2
(L-Pro-L-Pro-Gly)5-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
(Pro-Ala-Pro-Lys)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
n: 3,10
-
?
(Pro-Ala-Pro-Lys)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
n: 1-10, recombinant enzyme, (Pro-Ala-Pro-Lys)10 is a particularly good substrate
-
?
(Pro-Glu-Pro-Pro-Ala)5 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
-
?
(Pro-Glu-Pro-Pro-Ala)5 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
recombinant enzyme
-
?
(Pro-Gly-Pro)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
active substrate
-
?
(Pro-Gly-Pro)n + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
active substrate
-
?
(Pro-Pro-Gly)10 + 2-oxoglutarate + O2
? + succinate + CO2
-
-
-
-
?
(Pro-Pro-Gly)10 + 2-oxoglutarate + O2
? + succinate + CO2
-
-
-
?
(Pro-Pro-Gly)10 L-proline + 2-oxoglutarate + O2
(Pro-Pro-Gly)10 trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
(Pro-Pro-Gly)10 L-proline + 2-oxoglutarate + O2
(Pro-Pro-Gly)10 trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
(Pro-Pro-Gly)10 L-proline + 2-oxoglutarate + O2
(Pro-Pro-Gly)10 trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
(Pro-Pro-Gly)10 L-proline + 2-oxoglutarate + O2
(Pro-Pro-Gly)10 trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
(Pro-Pro-Gly)10 L-proline + 2-oxoglutarate + O2
(Pro-Pro-Gly)10 trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
(Pro-Pro-Gly)10 L-proline + 2-oxoglutarate + O2
(Pro-Pro-Gly)10 trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
(Pro-Pro-Gly)10 L-proline + 2-oxoglutarate + O2
(Pro-Pro-Gly)10 trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
(Pro-Pro-Gly)10 L-proline + 2-oxoglutarate + O2
(Pro-Pro-Gly)10 trans-4-hydroxy-L-proline + succinate + CO2
Paramecium bursaria Chlorella virus-1
-
-
-
-
?
(Pro-Pro-Gly)2 L-proline + 2-oxoglutarate + O2
(Pro-Pro-Gly)2 trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
(Pro-Pro-Gly)2 L-proline + 2-oxoglutarate + O2
(Pro-Pro-Gly)2 trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
the enzyme acts in (Pro-Pro-Gly)10 preferentially on prolines in Y positions in the X-Y-Gly triplets
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
-
-
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 5,10, poor substrates
-
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
-
-
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
a low hydroxylation rate is found with denatured (Pro-Pro-Gly)10
-
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 20
n: 20, n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 20
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
structural requirement for proline hydroxylation in collagen and related peptides: supersecondary structure, consisting of PP-II followed by a beta-turn, as the conformational determinant for proline hydroxylation in nascent collagen and related substrates of the enzyme, in elastin peptides, the beta-structure appears to substitute for the PP-II structure
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
recombinant enzyme
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Pro-Pro-Gly)n + 2-oxoglutarate + O2
(Pro-4-hydroxy-Pro-Gly)n + succinate + CO2
-
n: 1,5,10
n: 1,5,10
?
(Ser-Pro-Lys-Pro-Pro)5 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
-
?
(Ser-Pro-Lys-Pro-Pro)5 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
recombinant enzyme, (Ser-Pro-Lys-Pro)5 is a particularly good substrate
-
?
2-oxoglutarate + O2 + ascorbate
succinate + dehydroascorbate + CO2 + H2O
-
-
-
-
?
2-oxoglutarate + O2 + ascorbate
succinate + dehydroascorbate + CO2 + H2O
-
-
-
?
2-oxoglutarate + O2 + ascorbate
succinate + dehydroascorbate + CO2 + H2O
-
-
-
?
2-oxoglutarate + O2 + ascorbate
succinate + dehydroascorbate + CO2 + H2O
-
-
-
-
?
2-oxoglutarate + O2 + ascorbate
succinate + dehydroascorbate + CO2 + H2O
-
uncoupled oxidative decarboxylation
-
?
2-oxoglutarate + O2 + ascorbate
succinate + dehydroascorbate + CO2 + H2O
-
uncoupled oxidative decarboxylation
-
?
2-oxoglutarate + O2 + ascorbate
succinate + dehydroascorbate + CO2 + H2O
-
uncoupled oxidative decarboxylation
-
?
2-oxoglutarate + O2 + ascorbate
succinate + dehydroascorbate + CO2 + H2O
-
-
-
?
2-oxoglutarate + O2 + ascorbate
succinate + dehydroascorbate + CO2 + H2O
-
-
-
?
2-oxoglutarate + O2 + ascorbate
succinate + dehydroascorbate + CO2 + H2O
-
-
-
?
2-oxoglutarate + O2 + ascorbate
succinate + dehydroascorbate + CO2 + H2O
Paramecium bursaria Chlorella virus-1
-
-
-
-
?
carboxymethylated collagen L-proline + 2-oxoglutarate + O2
carboxymethylated collagen-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
carboxymethylated collagen L-proline + 2-oxoglutarate + O2
carboxymethylated collagen-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
Gly-Pro8 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide
-
96% relative activity with respect to poly(L-proline) of MW 2000
-
?
Gly-Pro8 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide
-
96% relative activity with respect to poly(L-proline) of MW 2000
-
?
His10-rSkp1A + ?
?
-
-
-
?
His10-rSkp1A + ?
?
-
-
-
?
hypoxia-inducible factor alpha L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor alpha trans-4-hydroxy-L-proline + succinate + CO2
isoform EGLN1 acts upon both the N-and the C-terminal oxygen-dependent degradation domain to target hypoxia-inducible factor alpha for proteasomal degradation
-
-
?
hypoxia-inducible factor alpha L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor alpha trans-4-hydroxy-L-proline + succinate + CO2
isoform EGLN2 acts upon both the N-and the C-terminal oxygen-dependent degradation domain to target hypoxia-inducible factor alpha for proteasomal degradation
-
-
?
hypoxia-inducible factor alpha L-proline + 2-oxoglutarate + O2
hypoxia-inducible factor alpha trans-4-hydroxy-L-proline + succinate + CO2
isoform EGLN3 acts on the N-terminal oxygen-dependent degradation domain
-
-
?
hypoxia-inducible factor L-proline + 2-oxoglutarate + O2
hypoxia inducible factor trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
hypoxia-inducible factor L-proline + 2-oxoglutarate + O2
hypoxia inducible factor trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
hypoxia-inducible factor L-proline + 2-oxoglutarate + O2
hypoxia inducible factor trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
hypoxia-inducible factor L-proline + 2-oxoglutarate + O2
hypoxia inducible factor trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
i.e. HIF, an alphabetaheterodimer, in which the stability of the alpha-subunit is regulated in an oxygen-dependent manner. Hydroxylation of one or two critical proline residues in the oxygen-dependent degradation domain leads to proteasomal degradation of the protein under normic conditions, while under hypoxic conditions the oxygen-requiring hydroxylation is inhibited and HIF-alpha escapes degradation and dimerizes with HIF-beta, overview
-
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
i.e. HIF
-
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
i.e. HIF, an alphabetaheterodimer, in which the stability of the alpha-subunit is regulated in an oxygen-dependent manner. Hydroxylation of one or two critical proline residues in the oxygen-dependent degradation domain leads to proteasomal degradation of the protein under normic conditions, while under hypoxic conditions the oxygen-requiring hydroxylation is inhibited and HIF-alpha escapes degradation and dimerizes with HIF-beta, overview
-
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
i.e. HIF
-
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
i.e. HIF, an alphabetaheterodimer, in which the stability of the alpha-subunti is regulated in an oxygen-dependent manner. Hydroxylation of one or two critical proline residues in the oxygen-dependent degradation domain leads to proteasomal degradation of the protein under normic conditions, while under hypoxic conditions the oxygen-requiring hydroxylation is inhibited and HIF-alpha escapes degradation and dimerizes with HIF-beta, overview
-
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
i.e. HIF, oxygen-dependent hydroxylation of proline residues in the alpha subunit of hypoxia-inducible transcription factor is central to the hypoxic response in animals. Prolyl hydroxylation of HIFalpha increases its binding to the von Hippel-Lindau protein, thus signaling for degradation via the ubiquitin-proteasome system
-
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
i.e. HIF
-
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
i.e. HIF, the substrate prolyl-residue is bound in a specific conformation and that a significant structural change involving a mobile loop likely occurs concomitant with HIFalpha binding. PHD catalysis involves the mobile region that isolates the hydroxylation site and stabilizes the PHD2-Fe2+-2OG complex. The hydroxylation sites of both NODD and CODD of HIFalpha occur within a conserved LXXLAP motif. In the tPHD2-CODD structure, Leu559CODD, Leu562CODD, and Ala563CODD of the LXXLAP motif form part of the CODD310-helix and make hydrophobic interactions with tPHD2
-
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
i.e. HIF, an alphabetaheterodimer, in which the stability of the alpha-subunit is regulated in an oxygen-dependent manner. Hydroxylation of one or two critical proline residues in the oxygen-dependent degradation domain leads to proteasomal degradation of the protein under normic conditions, while under hypoxic conditions the oxygen-requiring hydroxylation is inhibited and HIF-alpha escapes degradation and dimerizes with HIF-beta, overview
-
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
i.e. HIF
-
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
i.e. HIF, an alphabetaheterodimer, in which the stability of the alpha-subunti is regulated in an oxygen-dependent manner. Hydroxylation of one or two critical proline residues in the oxygen-dependent degradation domain leads to proteasomal degradation of the protein under normic conditions, while under hypoxic conditions the oxygen-requiring hydroxylation is inhibited and HIF-alpha escapes degradation and dimerizes with HIF-beta, overview
-
-
?
hypoxia-inducible transcription factor + 2-oxoglutarate + O2
hypoxia-inducible transcription factor trans-4-hydroxy-L-proline + succinate + CO2
-
i.e. HIF
-
-
?
L-Pro-L-Pro-Gly + 2-oxoglutarate + O2
L-Pro-L-Pro-Gly-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
L-Pro-L-Pro-Gly + 2-oxoglutarate + O2
L-Pro-L-Pro-Gly-trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
r
L-proline + 2-oxoglutarate + O2
4-hydroxyproline + succinate + CO2
-
2-oxoglutarate is essential for hydroxylation
-
?
L-proline + 2-oxoglutarate + O2
4-hydroxyproline + succinate + CO2
-
2-oxoglutarate is essential for hydroxylation
-
?
octa-L-proline + 2-oxoglutarate + O2
4-hydroxyproline containing peptide
-
81.8% relative activity with respect to poly(L-proline) of MW 2000
-
?
octa-L-proline + 2-oxoglutarate + O2
4-hydroxyproline containing peptide
-
81.8% relative activity with respect to poly(L-proline) of MW 2000
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
recombinant enzyme
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
-
do not serve as substrate, assayed with recombinant enzyme
-
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
-
MW 2000, 6000 and 12000
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
-
MW 2000, 6000 and 12000
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
-
-
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
-
MW 7000
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
-
Mr of poly(L-Pro) is about 5000
-
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
-
-
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
MW: 7000 and 44000
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
-
-
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
-
recombinant enzyme
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
-
-
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
-
-
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
-
-
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(4-hydroxyproline) + succinate + CO2
-
-
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(trans-4-hydroxy-L-proline) + succinate + CO2
-
Mr 30000-40000 Da, 15% of the activity with (L-Pro-L-Glu-L-Pro-L-Pro-L-Ala)5 L-proline
-
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(trans-4-hydroxy-L-proline) + succinate + CO2
-
Mr 5000-10000 Da, 5, 24% of the activity with (L-Pro-L-Glu-L-Pro-L-Pro-L-Ala)5 L-proline
-
-
?
poly(L-Pro) + 2-oxoglutarate + O2
poly(trans-4-hydroxy-L-proline) + succinate + CO2
-
-
-
-
?
poly(L-proline) + 2-oxoglutarate + O2
poly(trans-4-hydroxy-L-proline) + succinate + CO2
-
-
-
-
r
poly(L-proline) + 2-oxoglutarate + O2
poly(trans-4-hydroxy-L-proline) + succinate + CO2
poly(L-proline) with Mr 10000-2000
-
-
r
poly(L-proline) + 2-oxoglutarate + O2
poly(trans-4-hydroxy-L-proline) + succinate + CO2
poly(L-proline) with Mr 5000-1000
-
-
r
poly(L-proline) + 2-oxoglutarate + O2
poly(trans-4-hydroxy-L-proline) + succinate + CO2
-
-
-
-
r
poly(L-proline) + 2-oxoglutarate + O2
poly(trans-4-hydroxy-L-proline) + succinate + CO2
-
poly(L-proline) with Mr 40000
-
-
r
poly(L-proline) + 2-oxoglutarate + O2
poly(trans-4-hydroxy-L-proline) + succinate + CO2
-
poly(L-proline) with Mr 13000
-
-
r
poly(L-proline) + 2-oxoglutarate + O2
poly(trans-4-hydroxy-L-proline) + succinate + CO2
-
-
-
-
r
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-(2S,4R)-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-(2S,4R)-4-hydroxy-L-proline + succinate + CO2
-
prolyl 4-hydroxylase is a nonheme iron dioxygenase that catalyzes the posttranslational hydroxylation of (2S)-Pro residues in protocollagen strands
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
Q81LZ8
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
Q81LZ8
substrate binding and active site structure, overview
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
the enzyme preferentially recognizes the cis conformation of the prolyl peptide bond
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
key enzyme in collagen biosynthesis, catalyzes the conversion of selected prolyl residues to trans-hydroxyproline in nascent or completed pro-alpha chains of procollagen
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
the biological substrate for the enzyme is a proline residue in an appropriate sequence of a growing or newly synthesized polypeptide chain
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
key enzyme in collagen biosynthesis, catalyzes the conversion of selected prolyl residues to trans-hydroxyproline in nascent or completed pro-alpha chains of procollagen
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
the biological substrate for the enzyme is a proline residue in an appropriate sequence of a growing or newly synthesized polypeptide chain
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
acts on -Xaa-Pro-Gly triplets in collagen
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
P4H catalyzes the post-translational hydroxylation of proline residues in protocollagen strands, stabilizing the ensuing triple helix
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
high stringency for the iron-binding residues in the P4H active site, structure-function relationship, overview
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
PxGP (where x is not a proline) is the common motif of proline-rich peptide sequences that bind with high affinity to the enzyme (PSB-II)
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
the enzyme preferentially recognizes the cis conformation of the prolyl peptide bond
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
Paramecium bursaria Chlorella virus-1
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
the binding affinity of 2-oxoglutarate to PcP4H1 is very low
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
the binding affinity of 2-oxoglutarate to PcP4H1 is very low
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
procollagen L-proline + 2-oxoglutarate + O2
procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
-
-
?
proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
-
-
?
proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
synthetic peptides
-
?
proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
chelation to the enzyme-bound metal ion is important for proper binding of the substrate 2-oxoglutarate
-
?
proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
no hydroxylation of free proline, minimum sequence required X-Pro-Gly, best substrates are those where Pro precedes Gly, which can be substituted by Ala or beta-alanine. The amino acid preceding Pro can be Pro, Ala, Leu, Arg, Val, Glu, but not Gly or Ser. Additionally the sequence, the conformation and the peptide chain length influence the rate of hydroxylation
-
?
proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
the presence of 2-oxoglutarate is an absolute and highly specific requirement, the formation of 4-hydroxyproline is accompanied by a stoichiometric decarboxylation of 2-oxoglutarate, the oxygen of the hydroxyl group is derived from molecular oxygen, the other atom of the O2 molecule being incorporated into the succinate, the activated form of oxygen is probably superoxide
-
?
proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
the presence of 2-oxoglutarate is an absolute and highly specific requirement, the formation of 4-hydroxyproline is accompanied by a stoichiometric decarboxylation of 2-oxoglutarate, the oxygen of the hydroxyl group is derived from molecular oxygen, the other atom of the O2 molecule being incorporated into the succinate, the activated form of oxygen is probably superoxide
-
-
?
proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
-
-
?
proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
no hydroxylation of free proline, minimum sequence required X-Pro-Gly, best substrates are those where Pro precedes Gly, which can be substituted by Ala or beta-alanine. The amino acid preceding Pro can be Pro, Ala, Leu, Arg, Val, Glu, but not Gly or Ser. Additionally the sequence, the conformation and the peptide chain length influence the rate of hydroxylation
-
?
proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
the presence of 2-oxoglutarate is an absolute and highly specific requirement, the formation of 4-hydroxyproline is accompanied by a stoichiometric decarboxylation of 2-oxoglutarate, the oxygen of the hydroxyl group is derived from molecular oxygen, the other atom of the O2 molecule being incorporated into the succinate, the activated form of oxygen is probably superoxide
-
?
proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
the presence of 2-oxoglutarate is an absolute and highly specific requirement, the formation of 4-hydroxyproline is accompanied by a stoichiometric decarboxylation of 2-oxoglutarate, the oxygen of the hydroxyl group is derived from molecular oxygen, the other atom of the O2 molecule being incorporated into the succinate, the activated form of oxygen is probably superoxide
-
-
?
proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
-
-
?
proline containing peptide + 2-oxoglutarate + O2
4-hydroxyproline containing peptide + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
2-oxoadipate can replace 2-oxoglutarate as cosubstrate
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
protocollagen + 2-oxoglutarate + O2
4-hydroxyproline containing protocollagen + succinate + CO2
-
-
-
?
tert-butyloxycarbonyl-Pro8 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide
-
91.4% relative activity with respect to poly(L-proline) of MW 2000
-
?
tert-butyloxycarbonyl-Pro8 + 2-oxoglutarate + O2
4-hydroxyproline containing peptide
-
91.4% relative activity with respect to poly(L-proline) of MW 2000
-
?
additional information
?
-
-
the enzyme preferentially hydroxylates proline residues preceding glycines in (X-Y-Gly)n peptides. Peptides representing the N- and C-terminal hydroxylation sites present in hypoxia-inducible transcription factor alpha also serve as substrates
-
-
?
additional information
?
-
the enzyme preferentially hydroxylates proline residues preceding glycines in (X-Y-Gly)n peptides. Peptides representing the N- and C-terminal hydroxylation sites present in hypoxia-inducible transcription factor alpha also serve as substrates
-
-
?
additional information
?
-
the enzyme preferentially hydroxylates proline residues preceding glycines in (X-Y-Gly)n peptides. Peptides representing the N- and C-terminal hydroxylation sites present in hypoxia-inducible transcription factor alpha also serve as substrates
-
-
?
additional information
?
-
the enzyme preferentially hydroxylates proline residues preceding glycines in (X-Y-Gly)n peptides. Peptides representing the N- and C-terminal hydroxylation sites present in hypoxia-inducible transcription factor alpha also serve as substrates
-
-
?
additional information
?
-
Q81LZ8
enzyme BaP4H recognizes and acts on peptidyl substrates but not free L-proline, using elements characteristic of an Fe(II)/2-oxoglutarate-dependent dioxygenases, substrate specifiicty analysis by mass spectrometry, fluorescence binding, x-ray crystallography, and docking experiments, overview. Enzyme BaP4H can hydroxylate unique peptidyl proline sites in collagen-derived peptides with asymmetric hydroxylation patterns. The cofactor-bound crystal structures of BaP4H reveal active site conformational changes that define open and closed forms and mimic 'ready' and 'product-released' states of the enzyme in the catalytic cycle. Free L-proline binds to Fe(II)-BaP4H, but the affinity is an order of magnitude lower than for the peptides. No activity with free L-proline
-
-
?
additional information
?
-
-
enzyme BaP4H recognizes and acts on peptidyl substrates but not free L-proline, using elements characteristic of an Fe(II)/2-oxoglutarate-dependent dioxygenases, substrate specifiicty analysis by mass spectrometry, fluorescence binding, x-ray crystallography, and docking experiments, overview. Enzyme BaP4H can hydroxylate unique peptidyl proline sites in collagen-derived peptides with asymmetric hydroxylation patterns. The cofactor-bound crystal structures of BaP4H reveal active site conformational changes that define open and closed forms and mimic 'ready' and 'product-released' states of the enzyme in the catalytic cycle. Free L-proline binds to Fe(II)-BaP4H, but the affinity is an order of magnitude lower than for the peptides. No activity with free L-proline
-
-
?
additional information
?
-
-
substrate and ligand binding structures, overview
-
-
?
additional information
?
-
-
no reaction with: free proline, prolyl peptides whose residues number is four or less
-
-
?
additional information
?
-
-
no reaction with: free proline, prolyl peptides whose residues number is four or less
-
-
?
additional information
?
-
-
protocollagen and triple-helical (Pro-Pro-Gly)10 do not serve as substrate. 2-oxoadipate, 2-oxosuccinate or 2-oxovalerate do not replace 2-oxoglutarate
-
-
?
additional information
?
-
-
substrate and ligand binding structures, overview
-
-
?
additional information
?
-
-
substrate specificity, overview. The substrate is bound in a lefthanded (poly)-L-proline type II conformation in a tunnel shaped by two loops, mode of binding does not depend on stacking interactions of the proline sidechains with aromatic residues, substrate binding structure, modelling, overview. Major conformational changes of the two peptide binding loops are predicted to be a key feature of the catalytic cycle. These conformational changes are probably triggered by the conformational switch of Tyr140, as induced by the hydroxylation of the proline residue
-
-
?
additional information
?
-
-
no reaction with: free proline, prolyl peptides whose residues number is four or less
-
-
?
additional information
?
-
-
P4H1 modifies Skp1, an adaptor of the SCF class of E3-Ub ligases
-
-
?
additional information
?
-
-
substrate and ligand binding structures, overview
-
-
?
additional information
?
-
-
the enzyme is specific for proline in the second position after glycine, the position in which the hydroxyproline in collagen is found. No reaction with: free proline, glycyl-L-prolyl-L-proline or poly-L-proline II with a molecular weight of about 15000
-
-
?
additional information
?
-
-
thermal denaturing of the triple-helical conformation of the substrate before hydroxylation
-
-
?
additional information
?
-
-
thermal denaturing of the triple-helical conformation of the substrate before hydroxylation
-
-
?
additional information
?
-
-
thermal denaturing of the triple-helical conformation of the substrate before hydroxylation
-
-
?
additional information
?
-
-
thermal denaturing of the triple-helical conformation of the substrate before hydroxylation
-
-
?
additional information
?
-
-
thermal denaturing of the triple-helical conformation of the substrate before hydroxylation
-
-
?
additional information
?
-
-
thermal denaturing of the triple-helical conformation of the substrate before hydroxylation
-
-
?
additional information
?
-
-
thermal denaturing of the triple-helical conformation of the substrate before hydroxylation
-
-
?
additional information
?
-
-
thermal denaturing of the triple-helical conformation of the substrate before hydroxylation
-
-
?
additional information
?
-
-
thermal denaturing of the triple-helical conformation of the substrate before hydroxylation
-
-
?
additional information
?
-
-
the presence of lysyl hydroxylase in the reaction mixture has no effect on the activity of the enzyme
-
-
?
additional information
?
-
-
characterization of the 2-oxoglutarate binding site of the enzyme, 2-oxosuccinate, 2-oxovalerate, 2-oxobutyrate, 3-oxoglutarate or pyridine 2,5-dicarboxylate do not replace 2-oxoglutarate as cosubstrates
-
-
?
additional information
?
-
-
in the absence of a peptidylproline substrate, the oxidative decarboxylation of 2-oxoglutarate by the enzyme is stoichiometrically coupled to the oxidation of ascorbate
-
-
?
additional information
?
-
-
no substrate: prolines in recombinant type I procollagen chains
-
-
?
additional information
?
-
-
HIF prolyl hydroxylases are related to the collagen prolyl hydroxylases, but form unusually stable complexes with their Fe2+ cofactor and 2-oxoglutarate cosubstrate
-
-
?
additional information
?
-
-
C-P4H catalyses proline hydroxylation of collagens in the X-Pro-Gly (X-P-G) triplets
-
-
?
additional information
?
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the carboxy group of 2-oxoglutarate is bound by Lys493 in subunit alphaI, substrate and ligand binding structures, overview
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the heat shock protein 90 (HSP90) co-chaperones p23 and FKBP38 interact via a conserved Pro-Xaa-Leu-Glu motif in these proteins with the N-terminal Myeloid Nervy and DEAF-1 (MYND)-type zinc finger of PHD2
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prolyl-4-hydroxylase (P4H) is a non-heme iron hydroxylase that regio- and stereospecifically hydroxylates proline residues in a peptide chain into R-4-hydroxyproline. In P4H, a strong aliphatic C-H bond is activated, while thermodynamically much weaker aliphatic C-H groups, that is, at the C3 and C5 positions, are untouched
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additional information
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prolyl-4-hydroxylase (P4H) is a non-heme iron hydroxylase that regio- and stereospecifically hydroxylates proline residues in a peptide chain into R-4-hydroxyproline. In P4H, a strong aliphatic C-H bond is activated, while thermodynamically much weaker aliphatic C-H groups, that is, at the C3 and C5 positions, are untouched
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no reaction with: free proline, prolyl peptides whose residues number is four or less
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the enzyme clearly prefers X position proline to Y position proline in the sequences of (Gly-Pro-Ala)n versus (Gly-Ala-Pro)n
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substrate and ligand binding structures, overview
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no activity with poly-L-proline or the unhydroxylated decapeptide analog (Ala-Lys-Pro-Ser-Tyr-Pro-Pro-Thr-Tyr-Lys) of the polyphenolic protein
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molecular mechanism of intracellular degradation of type I collagen in normal corneal endothelial cells, role of the enzyme and protein-disulfide isomerase, which is the beta subunit of the enzyme, during procollagen I biosynthesis
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effect of substrate on activity
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thermal denaturing of the triple-helical conformation of the substrate before hydroxylation
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HPH isoforms are involved in infection of hosts and stress response
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thermal denaturing of the triple-helical conformation of the substrate before hydroxylation
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substrate and ligand binding structures, overview
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the BH4 domain is required for the interaction of PHD3 with Bcl-2, PHD3 promotes apoptosis via its BH4 domain
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thermal denaturing of the triple-helical conformation of the substrate before hydroxylation
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2-oxoglutarate cannot be replaced by oxalylglycine, 2-oxopentanoate, 2-oxoadipate, pyruvate or 2-oxomalonate
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2-oxoglutarate cannot be replaced by oxalylglycine, 2-oxopentanoate, 2-oxoadipate, pyruvate or 2-oxomalonate
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proline or the dipeptides Ser-Pro or Ala-Pro do not serve as substrates
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