Any feedback?
No. of entries
Information on EC 1.3.1.110 - lactate dehydrogenase (NAD+, ferredoxin)
for references in articles please use BRENDA:EC1.3.1.110
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 1 Oxidoreductases
1.3 Acting on the CH-CH group of donors
1.3.1 With NAD+ or NADP+ as acceptor
1.3.1.110 lactate dehydrogenase (NAD+, ferredoxin)
IUBMB Comments
The enzyme, isolated from the bacterium Acetobacterium woodii, uses flavin-based electron confurcation to drive endergonic lactate oxidation with NAD+ as oxidant at the expense of simultaneous exergonic electron flow from reduced ferredoxin to NAD+.
The expected taxonomic range for this enzyme is: Acetobacterium woodii
- 1.3.1.110
-
perfringens
-
enterotoxin
-
pastoral
-
supervisor
-
carbapenemase-producing
- carbapenemase
-
non-food-borne
Reaction Schemes
show+
2
+
2
=
+
2
+
2
+
2
+
2
reduced ferredoxin [iron-sulfur] cluster
=
+
2
+
2
oxidized ferredoxin [iron-sulfur] cluster
Synonyms
ldh/etf complex, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
LDH/Etf complex
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
lactate + 2 NAD+ + 2 reduced ferredoxin [iron-sulfur] cluster = pyruvate + 2 NADH + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
lactate:NAD+, ferredoxin oxidoreductase
The enzyme, isolated from the bacterium Acetobacterium woodii, uses flavin-based electron confurcation to drive endergonic lactate oxidation with NAD+ as oxidant at the expense of simultaneous exergonic electron flow from reduced ferredoxin to NAD+.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
lactate + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
pyruvate + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
lactate + 2 NAD+ + 2 reduced ferredoxin [iron-sulfur] cluster
pyruvate + 2 NADH + 2 oxidized ferredoxin [iron-sulfur] cluster
-
Substrates: -
Products: -
Products: -
?
pyruvate + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
lactate + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
lactate + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
pyruvate + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
Substrates: lactate is a common substrate for major groups of strictly anaerobic bacteria. The LDH/Etf complex of Acetobacterium woodii uses flavin-based electron confurcation to drive endergonic lactate oxidation with NAD+ as oxidant at the expense of simultaneous exergonic electron flow from reduced ferredoxin to NAD+
Products: -
Products: -
r
lactate + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
pyruvate + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
Substrates: pyruvate reduction to lactate with NADH as electron donor is highly exergonic
Products: -
Products: -
r
lactate + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
pyruvate + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
Substrates: lactate is a common substrate for major groups of strictly anaerobic bacteria. The LDH/Etf complex of Acetobacterium woodii uses flavin-based electron confurcation to drive endergonic lactate oxidation with NAD+ as oxidant at the expense of simultaneous exergonic electron flow from reduced ferredoxin to NAD+
Products: -
Products: -
r
lactate + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
pyruvate + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
Substrates: pyruvate reduction to lactate with NADH as electron donor is highly exergonic
Products: -
Products: -
r
pyruvate + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
lactate + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
Substrates: no NADH oxidation with pyruvate as electron acceptor. Only when oxidized ferredoxin is added to the system, the reaction is initiated and NADH oxidation is detected by a decrease of absorbance. NADH-dependent ferredoxin reduction is strictly dependent on the presence of lactate
Products: -
Products: -
r
pyruvate + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
lactate + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
Substrates: no NADH oxidation with pyruvate as electron acceptor. Only when oxidized ferredoxin is added to the system, the reaction is initiated and NADH oxidation is detected by a decrease of absorbance. NADH-dependent ferredoxin reduction is strictly dependent on the presence of lactate
Products: -
Products: -
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
lactate + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
pyruvate + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
lactate + 2 NAD+ + 2 reduced ferredoxin [iron-sulfur] cluster
pyruvate + 2 NADH + 2 oxidized ferredoxin [iron-sulfur] cluster
-
Substrates: -
Products: -
Products: -
?
lactate + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
pyruvate + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
Substrates: lactate is a common substrate for major groups of strictly anaerobic bacteria. The LDH/Etf complex of Acetobacterium woodii uses flavin-based electron confurcation to drive endergonic lactate oxidation with NAD+ as oxidant at the expense of simultaneous exergonic electron flow from reduced ferredoxin to NAD+
Products: -
Products: -
r
lactate + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
pyruvate + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
Substrates: lactate is a common substrate for major groups of strictly anaerobic bacteria. The LDH/Etf complex of Acetobacterium woodii uses flavin-based electron confurcation to drive endergonic lactate oxidation with NAD+ as oxidant at the expense of simultaneous exergonic electron flow from reduced ferredoxin to NAD+
Products: -
Products: -
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
the LDH/Etf complex has three predicted FADs. FAD is required for stability and activity. FAD (0.005 mM) is present during all purification steps, as the enzyme precipitates in the absence of FAD. FMN can not substitute FAD
[4Fe-4S]-center
the LDH/Etf complex has one predicted 4Fe-4S cluster
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CaCl2
divalent cations stimulate activity, highest stimulation observed with CaCl2 is twofold. Activity increased linearly with increasing CaCl2 concentration and reaches saturation at 40 mM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 9
activity is rather insensitive to a pH ranging from 5.5 to 9.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 50
10°C: 65% of maximal activity, activity is optimal between 20 and 30°C. Activity above 30°C decreases by 20% and dropps down to only residual activity at 50°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
H6LBB0: electron transfer flavoprotein beta subunit, H6LBB1: electron transfer flavoprotein alpha subunit, H6LBS1: D-lactate dehydrogenase subunit GlcD
UniProt
brenda
H6LBB0: electron transfer flavoprotein beta subunit, H6LBB1: electron transfer flavoprotein alpha subunit, H6LBS1: D-lactate dehydrogenase subunit GlcD
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
metabolism
metabolism
lactate is a common substrate for major groups of strictly anaerobic bacteria. The LDH/Etf complex of Acetobacterium woodii uses flavin-based electron confurcation to drive endergonic lactate oxidation with NAD+ as oxidant at the expense of simultaneous exergonic electron flow from reduced ferredoxin to NAD+
metabolism
-
lactate is a common substrate for major groups of strictly anaerobic bacteria. The LDH/Etf complex of Acetobacterium woodii uses flavin-based electron confurcation to drive endergonic lactate oxidation with NAD+ as oxidant at the expense of simultaneous exergonic electron flow from reduced ferredoxin to NAD+
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). LCTB_ACEWD
Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)
264
0
29069
Swiss-Prot
-
LCTC_ACEWD
Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)
418
0
46170
Swiss-Prot
-
LCTD_ACEWD
Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)
466
1
51142
Swiss-Prot
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
29000
1 * 51000 (D-lactate dehydrogenase glycolate oxidase subunit GlcD) + 1 * 46000 (electron transfer flavoprotein alpha subunit) + 1 * 29000 (electron transfer flavoprotein beta), SDS-PAGE
46000
1 * 51000 (D-lactate dehydrogenase glycolate oxidase subunit GlcD) + 1 * 46000 (electron transfer flavoprotein alpha subunit) + 1 * 29000 (electron transfer flavoprotein beta), SDS-PAGE
51000
1 * 51000 (D-lactate dehydrogenase glycolate oxidase subunit GlcD) + 1 * 46000 (electron transfer flavoprotein alpha subunit) + 1 * 29000 (electron transfer flavoprotein beta), SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotrimer
heterotrimer
1 * 51000 (D-lactate dehydrogenase glycolate oxidase subunit GlcD) + 1 * 46000 (electron transfer flavoprotein alpha subunit) + 1 * 29000 (electron transfer flavoprotein beta), SDS-PAGE
heterotrimer
-
1 * 51000 (D-lactate dehydrogenase glycolate oxidase subunit GlcD) + 1 * 46000 (electron transfer flavoprotein alpha subunit) + 1 * 29000 (electron transfer flavoprotein beta), SDS-PAGE
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Weghoff, M.C.; Bertsch, J.; Mller, V.
A novel mode of lactate metabolism in strictly anaerobic bacteria
Environ. Microbiol.
17
670-677
2015
Acetobacterium woodii (H6LBB0 and H6LBB1 and H6LBS1), Acetobacterium woodii, Acetobacterium woodii DSM 1030 (H6LBB0 and H6LBB1 and H6LBS1)
brenda
Buckel, W.; Thauer, R.
Flavin-based electron bifurcation, ferredoxin, flavodoxin, and anaerobic respiration with protons (Ech) or NAD+ (Rnf) as electron acceptors A historical review
Front. Microbiol.
9
401
2018
Acetobacterium woodii
brenda
EXTERNAL LINKS (specific for EC-Number 1.3.1.110)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
