Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.5.5.3 - hydroxyproline dehydrogenase and Organism(s) Homo sapiens

for references in articles please use BRENDA:EC1.5.5.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
A flavoprotein (FAD). The enzyme from human also has low activity with L-proline (cf. EC 1.5.5.2, proline dehydrogenase).
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Tetrapoda
Synonyms
hydroxyproline oxidase, hypdh, hydroxyproline dehydrogenase, oh-pox, proline dehydrogenase 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydroxyproline oxidase
HYPDH
OH-POX
ProDH2
proline dehydrogenase 2
-
PATHWAY SOURCE
PATHWAYS
-
-
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).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-proline + coenzyme Q1
?
show the reaction diagram
-
-
-
?
trans-4-hydroxy-L-proline + a quinone
(3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + a quinol
show the reaction diagram
-
-
-
-
?
trans-4-hydroxy-L-proline + coenzyme Q1
(3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + ?
show the reaction diagram
-
-
-
?
trans-4-hydroxy-L-proline + coenzyme Q10
(3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + ?
show the reaction diagram
preferred substrate
-
-
?
trans-4-hydroxy-L-proline + cytochrome c
(3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + reduced cytochrome c
show the reaction diagram
-
-
-
?
trans-4-hydroxy-L-proline + duroquinone
(3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + duroquinol
show the reaction diagram
-
-
-
?
trans-4-hydroxy-L-proline + menadione
(3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + menadiol
show the reaction diagram
-
-
-
?
trans-4-hydroxy-L-proline + menaquinone
(3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + menaquinol
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
trans-4-hydroxy-L-proline + a quinone
(3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + a quinol
show the reaction diagram
-
-
-
-
?
trans-4-hydroxy-L-proline + coenzyme Q10
(3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + ?
show the reaction diagram
preferred substrate
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1R,3R)-3-hydroxy-cyclopentane-carboxylate
-
5-hydroxy-1H-pyrazole-3-carboxylate
-
menadione
-
Tetrahydrofuroic acid
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.124
coenzyme Q1
at pH 7.5 and 25°C
0.143
duroquinone
at pH 7.5 and 25°C
0.025
menaquinone
at pH 7.5 and 25°C
200
trans-4-hydroxy-L-proline
at pH 7.5 and 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19
coenzyme Q1
at pH 7.5 and 25°C
0.27
duroquinone
at pH 7.5 and 25°C
0.28
menaquinone
at pH 7.5 and 25°C
0.19
trans-4-hydroxy-L-proline
at pH 7.5 and 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5
coenzyme Q1
at pH 7.5 and 25°C
1.9
duroquinone
at pH 7.5 and 25°C
75
L-proline
at pH 7.5 and 25°C
11
menaquinone
at pH 7.5 and 25°C
0.93
trans-4-hydroxy-L-proline
at pH 7.5 and 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.306
menadione
at pH 7.5 and 25°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.1
(1R,3R)-3-hydroxy-cyclopentane-carboxylate
Homo sapiens
at pH 7.5 and 25°C
2.9
5-hydroxy-1H-pyrazole-3-carboxylate
Homo sapiens
at pH 7.5 and 25°C
1.5
Tetrahydrofuroic acid
Homo sapiens
at pH 7.5 and 25°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme plays a role in growth regulation, reactive oxygen species generation, and activation of the apoptotic cascade
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HYPDH_HUMAN
536
0
58871
Swiss-Prot
Mitochondrion (Reliability: 2)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Q-Sepharose column chromatography and HisPur cobalt resin column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli C41(DE3) cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
adriamycin induces p53-mediated gene expression and markedly increases the catalytic activity of the enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
the enzyme is a therapeutic target for the treatment of primary hyperoxaluria
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team