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Information on EC 1.1.1.27 - L-lactate dehydrogenase and Organism(s) Champsocephalus gunnari and UniProt Accession O93541

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IUBMB Comments
Also oxidizes other (S)-2-hydroxymonocarboxylic acids. NADP+ also acts, more slowly, with the animal, but not the bacterial, enzyme.
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This record set is specific for:
Champsocephalus gunnari
UNIPROT: O93541
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The taxonomic range for the selected organisms is: Champsocephalus gunnari
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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(S)-lactate
+
NAD+
=
pyruvate
+
NADH
+
H+
+
=
+
+
Synonyms
lactate dehydrogenase, lactic dehydrogenase, ldh-a, lactate dehydrogenase a, l-lactate dehydrogenase, ldh-5, lactic acid dehydrogenase, ldh-1, pfldh, alpha-hydroxybutyrate dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydrogenase, lactate
-
-
-
-
Epsilon crystallin
-
-
-
-
epsilon-crystallin
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-
-
-
Immunogenic protein p36
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-
-
-
L(+)-nLDH
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-
-
-
L-(+)-lactate dehydrogenase
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-
-
-
L-lactic acid dehydrogenase
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-
-
-
L-lactic dehydrogenase
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-
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-
L-LDH
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-
-
-
lactate dehydrogenase
lactate dehydrogenase NAD-dependent
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-
-
lactic acid dehydrogenase
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-
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-
lactic dehydrogenase
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-
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-
NAD-lactate dehydrogenase
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-
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-
proteins, specific or class, anoxic stress response, p34
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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)-lactate:NAD+ oxidoreductase
Also oxidizes other (S)-2-hydroxymonocarboxylic acids. NADP+ also acts, more slowly, with the animal, but not the bacterial, enzyme.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-60-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
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
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
LDH catalyzes the conversion of pyruvate to lactate with concomitant oxidation of NADH during the last step in anaerobic glycolysis
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-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.16
pyruvate
pH 7.0, 0°C, recombinant enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
230
pyruvate
pH 7.0, 0°C, recombinant enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LDHA_CHAGU
331
0
36156
Swiss-Prot
other Location (Reliability: 3)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo enzyme form, X-ray diffraction structure determination and analysis at 2.35 A resolution, molecular replacement
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
inactivation above, thermal stability in relation to enzyme structure comparison to enzymes from other species in extreme environments
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme by ultracentrifugation, hydrophobic interaction chromatography, gel filtration, and ultrafiltration
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Coquelle, N.; Fioravanti, E.; Weik, M.; Vellieux, F.; Madern, D.
Activity, stability and structural studies of lactate dehydrogenases adapted to extreme thermal environments
J. Mol. Biol.
374
547-562
2007
Champsocephalus gunnari (O93541), Champsocephalus gunnari, Deinococcus radiodurans (P50933), Deinococcus radiodurans, Thermus thermophilus (Q5SJA1), Thermus thermophilus
Manually annotated by BRENDA team