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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.3.2.3 - L-galactonolactone dehydrogenase and Organism(s) Brassica oleracea and UniProt Accession O47881

for references in articles please use BRENDA:EC1.3.2.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
This enzyme catalyses the final step in the biosynthesis of L-ascorbic acid in higher plants and in nearly all higher animals with the exception of primates and some birds . The enzyme is very specific for its substrate L-galactono-1,4-lactone as D-galactono-gamma-lactone, D-gulono-gamma-lactone, L-gulono-gamma-lactone, D-erythronic-gamma-lactone, D-xylonic-gamma-lactone, L-mannono-gamma-lactone, D-galactonate, D-glucuronate and D-gluconate are not substrates . FAD, NAD+, NADP+ and O2 (cf. EC 1.3.3.12, L-galactonolactone oxidase) cannot act as electron acceptor .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Brassica oleracea
UNIPROT: O47881
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: Brassica oleracea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
l-galactono-1,4-lactone dehydrogenase, galldh, l-galactono-gamma-lactone dehydrogenase, ferricytochrome c oxidoreductase, l-galldh, gldhase, galactono-1,4-lactone dehydrogenase, gldase, l-galactonolactone dehydrogenase, galactonolactone dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydrogenase, galactonolactone
-
-
-
-
L-galactono-gamma-lactone dehydrogenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-galactono-1,4-lactone:ferricytochrome-c oxidoreductase
This enzyme catalyses the final step in the biosynthesis of L-ascorbic acid in higher plants and in nearly all higher animals with the exception of primates and some birds [5]. The enzyme is very specific for its substrate L-galactono-1,4-lactone as D-galactono-gamma-lactone, D-gulono-gamma-lactone, L-gulono-gamma-lactone, D-erythronic-gamma-lactone, D-xylonic-gamma-lactone, L-mannono-gamma-lactone, D-galactonate, D-glucuronate and D-gluconate are not substrates [5]. FAD, NAD+, NADP+ and O2 (cf. EC 1.3.3.12, L-galactonolactone oxidase) cannot act as electron acceptor [5].
CAS REGISTRY NUMBER
COMMENTARY hide
9029-02-1
-
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GLDH_BRAOL
600
0
67830
Swiss-Prot
Mitochondrion (Reliability: 2)