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Information on EC 1.1.1.441 - polyprenol dehydrogenase [NAD(P)H]
for references in articles please use BRENDA:EC1.1.1.441
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.441 polyprenol dehydrogenase [NAD(P)H]
IUBMB Comments
The enzyme, present in all eukaryotes, catalyses the dehydrogenation of ditrans,polycis-polyprenol and the reduction of dolichal as part of the pathway that converts ditrans,polycis-polyprenol to dolichol (cf. 1.3.1.94, polyprenal reductase). The enzyme works equally well with NAD+ and NADP+, but due to the cellular ratios of NAD+/NADH and NADP+/NADPH, the enzyme catalyses the oxidation of of polyprenol using NAD+ as the electron acceptor, and the reduction of dolichal using NADPH as the electron donor.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showa ditrans,polycis-polyprenol
+
=
a ditrans,polycis-polyprenal
+
+
+
=
a dolichal
+
+
Synonyms
chDHRSX, DHRSX, dolichal reductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DHRSX
dolichal reductase
-
-
-
-
DHRSX
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a ditrans,polycis-polyprenol + NAD(P)+ = a ditrans,polycis-polyprenal + NAD(P)H + H+
(1)
-
-
-
a dolichol + NAD(P)+ = a dolichal + NAD(P)H + H+
(2)
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ditrans,polycis-polyprenol:NAD(P)+ oxidoreductase
The enzyme, present in all eukaryotes, catalyses the dehydrogenation of ditrans,polycis-polyprenol and the reduction of dolichal as part of the pathway that converts ditrans,polycis-polyprenol to dolichol (cf. 1.3.1.94, polyprenal reductase). The enzyme works equally well with NAD+ and NADP+, but due to the cellular ratios of NAD+/NADH and NADP+/NADPH, the enzyme catalyses the oxidation of of polyprenol using NAD+ as the electron acceptor, and the reduction of dolichal using NADPH as the electron donor.
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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
dolichal + NAD(P)H + H+
dolichol + NADP+
Substrates: the enzyme works equally well with NAD+ and NADP+, but due to the cellular ratios of NAD+/NADH and NADP+/NADPH, the enzyme catalyses the reduction of dolichal using NADPH as the electron donor
Products: -
Products: -
?
polyprenol-18 + NAD+
polyprenal-18 + NADH + H+
Substrates: -
Products: -
Products: -
?
polyprenol-18 + NADP+
polyprenal-18 + NADPH + H+
Substrates: -
Products: -
Products: -
?
polyprenol-19 + NAD+
polyprenal-19 + NADH + H+
Substrates: -
Products: -
Products: -
?
polyprenol-19 + NADP+
polyprenal-19 + NADPH + H+
Substrates: -
Products: -
Products: -
?
ditrans,polycis-polyprenol + NAD+
ditrans,polycis-polyprenal + NADH + H+
-
Substrates: -
Products: -
Products: -
?
ditrans,polycis-polyprenol + NAD+
ditrans,polycis-polyprenal + NADH + H+
Substrates: the enzyme works equally well with NAD+ and NADP+, but due to the cellular ratios of NAD+/NADH and NADP+/NADPH, the enzyme catalyses the oxidation of of polyprenol using NAD+ as the electron acceptor
Products: -
Products: -
?
ditrans,polycis-polyprenol + NAD+
ditrans,polycis-polyprenal + NADH + H+
Substrates: the enzyme works equally well with NAD+ and NADP+, but due to the cellular ratios of NAD+/NADH and NADP+/NADPH, the enzyme catalyses the oxidation of polyprenol using NAD+ as the electron acceptor
Products: -
Products: -
?
ditrans,polycis-polyprenol + NADP+
ditrans,polycis-polyprenal + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
ditrans,polycis-polyprenol + NADP+
ditrans,polycis-polyprenal + NADPH + H+
Substrates: the enzyme works equally well with NAD+ and NADP+, but due to the cellular ratios of NAD+/NADH and NADP+/NADPH, the enzyme catalyses the oxidation of polyprenol using NAD+ as the electron acceptor
Products: -
Products: -
?
dolichal + NADH + H+
dolichol + NAD+
Substrates: the enzyme works equally well with NAD+ and NADP+, but due to the cellular ratios of NAD+/NADH and NADP+/NADPH, the enzyme catalyses the reduction of dolichal using NADPH as the electron donor
Products: -
Products: -
?
dolichal + NADPH + H+
dolichol + NADP+
Substrates: the enzyme works equally well with NAD+ and NADP+, but due to the cellular ratios of NAD+/NADH and NADP+/NADPH, the enzyme catalyses the reduction of dolichal using NADPH as the electron donor
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
ditrans,polycis-polyprenol + NADP+
ditrans,polycis-polyprenal + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
ditrans,polycis-polyprenol + NAD+
ditrans,polycis-polyprenal + NADH + H+
-
Substrates: -
Products: -
Products: -
?
ditrans,polycis-polyprenol + NAD+
ditrans,polycis-polyprenal + NADH + H+
Substrates: the enzyme works equally well with NAD+ and NADP+, but due to the cellular ratios of NAD+/NADH and NADP+/NADPH, the enzyme catalyses the oxidation of of polyprenol using NAD+ as the electron acceptor
Products: -
Products: -
?
dolichal + NADPH + H+
dolichol + NADP+
Substrates: the enzyme works equally well with NAD+ and NADP+, but due to the cellular ratios of NAD+/NADH and NADP+/NADPH, the enzyme catalyses the reduction of dolichal using NADPH as the electron donor
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
the enzyme works equally well with NAD+ and NADP+, but due to the cellular ratios of NAD+/NADH and NADP+/NADPH, the enzyme catalyses the oxidation of of polyprenol using NAD+ as the electron acceptor, and the reduction of dolichal using NADPH as the electron donor
NADH
the enzyme works equally well with NAD+ and NADP+, but due to the cellular ratios of NAD+/NADH and NADP+/NADPH, the enzyme catalyses the oxidation of of polyprenol using NAD+ as the electron acceptor, and the reduction of dolichal using NADPH as the electron donor
NADP+
the enzyme works equally well with NAD+ and NADP+, but due to the cellular ratios of NAD+/NADH and NADP+/NADPH, the enzyme catalyses the oxidation of of polyprenol using NAD+ as the electron acceptor, and the reduction of dolichal using NADPH as the electron donor
NADPH
the enzyme works equally well with NAD+ and NADP+, but due to the cellular ratios of NAD+/NADH and NADP+/NADPH, the enzyme catalyses the oxidation of of polyprenol using NAD+ as the electron acceptor, and the reduction of dolichal using NADPH as the electron donor
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
slight inhibition of the NADPH-dependent dolichal reductase activity
NADPH
slight inhibition of the NAD+-dependent polyprenol dehydrogenase activity
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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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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
malfunction
physiological function
the enzyme catalyzes two nonconsecutive steps in dolichol synthesis pathway using different cofactor. The enzyme catalyses the oxidation of of polyprenol using NAD+ as the electron acceptor, and the reduction of dolichal using NADPH as the electron donors
malfunction
-
absence of the dolichol synthesis gene DHRSX leads to N-glycosylation defects in Lec5 and Lec9 Chinese hamster ovary cells
malfunction
DHRSX deficiency leads to defective N-glycosylation by disrupting dolichol synthesis. Patients with missense variants in DHRSX (DHRSX-CDG) show a pseudoautosomal-recessive disease presenting as a congenital disorder of glycosylation
Show AA Sequence and Transmembrane Helices (576 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wilson, M.P.; Kentache, T.; Althoff, C.R.; Schulz, C.; de Bettignies, G.; Mateu Cabrera, G.; Cimbalistiene, L.; Burnyte, B.; Yoon, G.; Costain, G.; Vuillaumier-Barrot, S.; Cheillan, D.; Rymen, D.; Rychtarova, L.; Hansikova, H.; Bury, M.; Dewulf, J.P.; Caligiore, F.; Jaeken, J.; Cantagrel, V.; Va, V.a.n.
A pseudoautosomal glycosylation disorder prompts the revision of dolichol biosynthesis
Cell
187
3585-3601.e22
2024
Homo sapiens (Q8N5I4)
brenda
Kentache, T.; Althoff, C.R.; Caligiore, F.; Souche, E.; Schulz, C.; Graff, J.; Pieters, E.; Stanley, P.; Contessa, J.N.; Van Schaftingen, E.; Matthijs, G.; Foulquier, F.; Bommer, G.T.; Wilson, M.P.
Absence of the dolichol synthesis gene DHRSX leads to N-glycosylation defects in Lec5 and Lec9 Chinese hamster ovary cells
J. Biol. Chem.
300
107875
2024
Cricetulus griseus
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.441)
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Release 2026.1 (March 2026)
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