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Information on EC 1.2.1.22 - lactaldehyde dehydrogenase and Organism(s) Saccharolobus solfataricus and UniProt Accession Q97UA1

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Saccharolobus solfataricus
UNIPROT: Q97UA1 not found.
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The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The enzyme appears in selected viruses and cellular organisms
Synonyms
lactaldehyde dehydrogenase, l-lactaldehyde dehydrogenase, psladh, avladh, mj1411, nad-dependent lactaldehyde dehydrogenase, nicotinamide adenine dinucleotide (nad)-linked dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L-lactaldehyde dehydrogenase
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dehydrogenase, lactaldehyde
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L-lactaldehyde:NAD oxidoreductase
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Lactaldehyde dehydrogenase
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nicotinamide adenine dinucleotide (NAD)-linked dehydrogenase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
(S)-lactaldehyde:NAD+ oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
37250-90-1
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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
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
show the reaction diagram
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-
?
(S)-lactaldehyde + NADP+ + H2O
(S)-lactate + NADPH + 2 H+
show the reaction diagram
assay using NADP+
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-
?
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
(S)-lactaldehyde + NAD+ + H2O
(S)-lactate + NADH + 2 H+
show the reaction diagram
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
2,5-dioxopentanoate dehydrogenase, cf. EC 1.2.1.26
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme catalyzes the last step in the degradation of L-fucose
physiological function
the enzyme catalyzes the last step in the degradation of L-fucose. The activity with L-lactaldehyde is fivefold increased in L-fucose adapted cells compared with D-glucose. Only poor conversion of D-lactaldehyde under both conditions is observed
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wolf, J.; Stark, H.; Fafenrot, K.; Albersmeier, A.; Pham, T.K.; Mueller, K.B.; Meyer, B.H.; Hoffmann, L.; Shen, L.; Albaum, S.P.; Kouril, T.; Schmidt-Hohagen, K.; Neumann-Schaal, M.; Braesen, C.; Kalinowski, J.; Wright, P.C.; Albers, S.V.; Schomburg, D.; Siebers, B.
A systems biology approach reveals major metabolic changes in the thermoacidophilic archaeon Sulfolobus solfataricus in response to the carbon source L-fucose versus D-glucose
Mol. Microbiol.
102
882-908
2016
Saccharolobus solfataricus (Q97UA1), Saccharolobus solfataricus P2 (Q97UA1)
Manually annotated by BRENDA team