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Information on EC 1.5.5.3 - hydroxyproline dehydrogenase
for references in articles please use BRENDA:EC1.5.5.3
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EC Tree 1 Oxidoreductases
1.5 Acting on the CH-NH group of donors
1.5.5 With a quinone or similar compound as acceptor
1.5.5.3 hydroxyproline dehydrogenase
IUBMB Comments
A flavoprotein (FAD). The enzyme from human also has low activity with L-proline (cf. EC 1.5.5.2, proline dehydrogenase).
The expected taxonomic range for this enzyme is: Tetrapoda
- 1.5.5.3
- oxalate
- glycolate
- urinary
- hyperoxalurias
- glyoxylate
-
stone
- prodh2
- collagen
- aminotransferase
- dehydratase
- aldolase
-
inborn
-
infancy
-
hyperprolinemia
-
delta-1-pyrroline-5-carboxylate
-
schizophrenia
- grhpr
- medicine
Reaction Schemes
showSynonyms
hydroxyproline oxidase, hypdh, hydroxyproline dehydrogenase, oh-pox, proline dehydrogenase 2, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
hydroxyproline oxidase
HYPDH
OH-POX
ProDH2
hydroxyproline oxidase
-
-
-
-
HYPDH
-
-
-
-
OH-POX
-
-
-
-
ProDH2
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
trans-4-hydroxy-L-proline + a quinone = (3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + a quinol
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
trans-4-hydroxy-L-proline degradation I
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SYSTEMATIC NAME
IUBMB Comments
trans-4-hydroxy-L-proline:quinone oxidoreductase
A flavoprotein (FAD). The enzyme from human also has low activity with L-proline (cf. EC 1.5.5.2, proline dehydrogenase).
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
trans-4-hydroxy-L-proline + a quinone
(3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + a quinol
trans-4-hydroxy-L-proline + coenzyme Q1
(3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + ?
Substrates: -
Products: -
Products: -
?
trans-4-hydroxy-L-proline + coenzyme Q10
(3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + ?
Substrates: preferred substrate
Products: -
Products: -
?
trans-4-hydroxy-L-proline + cytochrome c
(3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + reduced cytochrome c
Substrates: -
Products: -
Products: -
?
trans-4-hydroxy-L-proline + duroquinone
(3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + duroquinol
Substrates: -
Products: -
Products: -
?
trans-4-hydroxy-L-proline + menadione
(3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + menadiol
Substrates: -
Products: -
Products: -
?
trans-4-hydroxy-L-proline + menaquinone
(3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + menaquinol
Substrates: -
Products: -
Products: -
?
trans-4-hydroxy-L-proline + O2
(3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + ?
-
Substrates: -
Products: -
Products: -
?
trans-4-hydroxy-L-proline + a quinone
(3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + a quinol
-
Substrates: -
Products: -
Products: -
?
trans-4-hydroxy-L-proline + a quinone
(3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + a quinol
-
Substrates: -
Products: -
Products: -
?
trans-4-hydroxy-L-proline + a quinone
(3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + a quinol
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with trans-4-hydroxy-D-proline, cis-4-hydroxy-L-proline, and cis-4-hydroxy-D-proline
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with trans-4-hydroxy-D-proline, cis-4-hydroxy-L-proline, and cis-4-hydroxy-D-proline
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is a poor oxidase using O2 as electron acceptor
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a poor oxidase using O2 as electron acceptor
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
trans-4-hydroxy-L-proline + a quinone
(3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + a quinol
trans-4-hydroxy-L-proline + coenzyme Q10
(3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + ?
Substrates: preferred substrate
Products: -
Products: -
?
trans-4-hydroxy-L-proline + O2
(3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + ?
-
Substrates: -
Products: -
Products: -
?
trans-4-hydroxy-L-proline + a quinone
(3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + a quinol
-
Substrates: -
Products: -
Products: -
?
trans-4-hydroxy-L-proline + a quinone
(3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + a quinol
-
Substrates: -
Products: -
Products: -
?
trans-4-hydroxy-L-proline + a quinone
(3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + a quinol
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
(1S,3R)-3-hydroxy-cyclopentane carboxylic acid, trans-4-hydroxy-D-proline, cis-4-hydroxy-L-proline, and cis-4-hydroxy-D-proline do not cause inhibition even up to 5 mM
-
additional information
-
(1S,3R)-3-hydroxy-cyclopentane carboxylic acid, trans-4-hydroxy-D-proline, cis-4-hydroxy-L-proline, and cis-4-hydroxy-D-proline do not cause inhibition even up to 5 mM
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Hyperoxaluria, Primary
Metabolism of (13)C5-hydroxyproline in mouse models of Primary Hyperoxaluria and its inhibition by RNAi therapeutics targeting liver glycolate oxidase and hydroxyproline dehydrogenase.
Hyperoxaluria, Primary
Proline dehydrogenase 2 (PRODH2) is a hydroxyproline dehydrogenase (HYPDH) and molecular target for treating primary hyperoxaluria.
Hyperoxaluria, Primary
Re: The Effects of the Inactivation of Hydroxyproline Dehydrogenase on Urinary Oxalate and Glycolate Excretion in Mouse Models of Primary Hyperoxaluria.
Hyperoxaluria, Primary
The effects of the inactivation of Hydroxyproline dehydrogenase on urinary oxalate and glycolate excretion in mouse models of primary hyperoxaluria.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
the enzyme plays a role in growth regulation, reactive oxygen species generation, and activation of the apoptotic cascade
physiological function
creation of a ProDH2 knock out mouse model. The lack of hydroxyproline dehydrogenase in primary hyperoxalurias mouse models results in lower levels of urinary oxalate excretion. In the double knockout mouse, lacking both glyoxylate reductase/hydroxypyruvate reductase Grhpr and ProDH2, calcium-oxalate crystal deposition in the kidney is prevented, when placed on a 1% hydroxyproline diet
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). HYPDH_BOVIN
461
0
51262
Swiss-Prot
Mitochondrion (Reliability: 1)
HYPDH_HUMAN
536
0
58871
Swiss-Prot
Mitochondrion (Reliability: 2)
HYPDH_MOUSE
456
0
50723
Swiss-Prot
Mitochondrion (Reliability: 4)
HYPDH_RAT
456
0
51002
Swiss-Prot
Mitochondrion (Reliability: 3)
HYPDH_XENLA
466
0
52329
Swiss-Prot
Mitochondrion (Reliability: 2)
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Q-Sepharose column chromatography and HisPur cobalt resin column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
adriamycin induces p53-mediated gene expression and markedly increases the catalytic activity of the enzyme
hydroxyproline oxidase expression is not increased in rats on a high-fat, carbohydrate-free diet
-
in rats, hydroxyproline oxidase activity is maximal in the suckling period
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
the enzyme is a therapeutic target for the treatment of primary hyperoxaluria
medicine
creation of a ProDH2 knock out mouse model. The lack of hydroxyproline dehydrogenase in primary hyperoxalurias mouse models results in lower levels of urinary oxalate excretion. In the double knockout mouse, lacking both glyoxylate reductase/hydroxypyruvate reductase Grhpr and ProDH2, calcium-oxalate crystal deposition in the kidney is prevented, when placed on a 1% hydroxyproline diet
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wu, Z.; Hou, Y.; Dai, Z.; Hu, C.A.; Wu, G.
Metabolism, nutrition, and redox signaling of hydroxyproline
Antioxid. Redox Signal.
30
674-682
2017
Homo sapiens
brenda
Summitt, C.B.; Johnson, L.C.; Joensson, T.J.; Parsonage, D.; Holmes, R.P.; Lowther, W.T.
Proline dehydrogenase 2 (PRODH2) is a hydroxyproline dehydrogenase (HYPDH) and molecular target for treating primary hyperoxaluria
Biochem. J.
466
273-281
2015
Homo sapiens (Q9UF12), Homo sapiens
brenda
Li, X.; Knight, J.; Fargue, S.; Buchalski, B.; Guan, Z.; Inscho, E.W.; Liebow, A.; Fitzgerald, K.; Querbes, W.; Todd Lowther, W.; Holmes, R.P.
Metabolism of (13)C5-hydroxyproline in mouse models of primary hyperoxaluria and its inhibition by RNAi therapeutics targeting liver glycolate oxidase and hydroxyproline dehydrogenase
Biochim. Biophys. Acta
1862
233-239
2016
Mus musculus
brenda
Carnie, J.A.; Rowsell, E.V.; Dabbaghian, M.K.; Hobbs, D.R.; Rowsell, K.V.
Comparative and developmental studies on 4-hydroxy-2-oxoglutarate aldolase and hydroxyproline oxidase
Comp. Biochem. Physiol. B
71
681-687
1982
Rattus norvegicus
brenda
Cooper, S.K.; Pandhare, J.; Donald, S.P.; Phang, J.M.
A novel function for hydroxyproline oxidase in apoptosis through generation of reactive oxygen species
J. Biol. Chem.
283
10485-10492
2008
Homo sapiens (Q9UF12)
brenda
Lowry, M.; Hall, D.E.; Brosnan, J.T.
Hydroxyproline metabolism by the rat kidney distribution of renal enzymes of hydroxyproline catabolism and renal conversion of hydroxyproline to glycine and serine
Metab. Clin. Exp.
34
955-961
1985
Rattus norvegicus
brenda
Buchalski, B.; Wood, K.D.; Challa, A.; Fargue, S.; Holmes, R.P.; Lowther, W.T.; Knight, J.
The effects of the inactivation of hydroxyproline dehydrogenase on urinary oxalate and glycolate excretion in mouse models of primary hyperoxaluria
Biochim. Biophys. Acta
1866
165633
2020
Mus musculus (Q8VCZ9), Mus musculus
brenda
EXTERNAL LINKS (specific for EC-Number 1.5.5.3)
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Release 2023.1 (January 2023)
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