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Information on EC 1.3.1.94 - polyprenol reductase and Organism(s) Homo sapiens and UniProt Accession Q9H8P0

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EC Tree
     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.1 With NAD+ or NADP+ as acceptor
                1.3.1.94 polyprenol reductase
IUBMB Comments
The reaction occurs in the reverse direction with reduction of the terminal double bond next to the alcohol group. Isolated from human fetal brain tissue but present in all eukaryotes. In mammalian cells dolichols are predominantly 18-21 isoprene units in length.
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This record set is specific for:
Homo sapiens
UNIPROT: Q9H8P0
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
srd5a3, polyprenol reductase, steroid 5alpha-reductase type 3, dfg10, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
steroid 5alpha-reductase type 3
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DFG10
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SRD5A3
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SYSTEMATIC NAME
IUBMB Comments
ditrans,polycis-dolichol:NADP+ 2,3-oxidoreductase
The reaction occurs in the reverse direction with reduction of the terminal double bond next to the alcohol group. Isolated from human fetal brain tissue but present in all eukaryotes. In mammalian cells dolichols are predominantly 18-21 isoprene units in length.
CAS REGISTRY NUMBER
COMMENTARY hide
116412-44-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ditrans,polycis-polyprenol + NADPH + H+
ditrans,polycis-dolichol + NADP+
show the reaction diagram
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
enzyme is necessary for the reduction of the alpha-isoprene unit of polyprenols to form dolichols, required for synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N-glycosylation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PORED_HUMAN
318
6
36521
Swiss-Prot
Secretory Pathway (Reliability: 3)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Saccharomyces cerevisiae and HEK-293T cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
loss of function mutations of the SRD5A3 gene cause a multisystemic syndrome with eye malformations, cerebellar vermis hypoplasia, and psychomotor delay. Plasma from patients shows increased level of polyprenoids
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cantagrel, V.; Lefeber, D.J.; Ng, B.G.; Guan, Z.; Silhavy, J.L.; Bielas, S.L.; Lehle, L.; Hombauer, H.; Adamowicz, M.; Swiezewska, E.; De Brouwer, A.P.; Bluemel, P.; Sykut-Cegielska, J.; Houliston, S.; Swistun, D.; Ali, B.R.; Dobyns, W.B.; Babovic-Vuksanovic, D.; van Bokhoven, H.; Wevers, R.A.; Raetz, C.
SRD5A3 is required for converting polyprenol to dolichol and is mutated in a congenital glycosylation disorder
Cell
142
203-217
2010
Homo sapiens (Q9H8P0), Homo sapiens, Mus musculus (Q9WUP4)
Manually annotated by BRENDA team