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Information on EC 1.1.1.27 - L-lactate dehydrogenase and Organism(s) Bifidobacterium longum and UniProt Accession P0CW93

for references in articles please use BRENDA:EC1.1.1.27
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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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Select one or more organisms in this record:
This record set is specific for:
Bifidobacterium longum
UNIPROT: P0CW93
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The taxonomic range for the selected organisms is: Bifidobacterium longum
Reaction Schemes
Synonyms
A4-LDH, AdhE, anaerobic lactate dehydrogenase, BbLDH, dehydrogenase, lactate, eLDHA, eLDHB, Epsilon crystallin, epsilon-crystallin, H4-L-lactate dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydrogenase, lactate
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Epsilon crystallin
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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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L-LDH
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lactate dehydrogenase
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lactate dehydrogenase NAD-dependent
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lactic acid dehydrogenase
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lactic dehydrogenase
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LDH
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NAD-lactate dehydrogenase
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proteins, specific or class, anoxic stress response, p34
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
fructose 1,6-diphosphate
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L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C210S
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crystallization of mutant enzyme
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
development of a recombinant yeast exhibiting efficient lactate production by substituting the coding region of PDC1 on chromosome XII for that of LDH through homologous recombination
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Iwata, S.; Yoshida, S.; Ohta, T.
A regular 1:1 complex of two allosteric states in the single crystal of L-lactate dehydrogenase from Bifidobacterium longum
J. Mol. Biol.
236
958-959
1994
Bifidobacterium longum
Manually annotated by BRENDA team
Iwata, S.; Kamata, K.; Yoshida, S.; Minowa, T.; Ohta, T.
T and R states in the crystals of bacterial L-lactate dehydrogenase reveal the mechanism for allosteric control
Nat. Struct. Biol.
1
176-185
1994
Bifidobacterium longum
Manually annotated by BRENDA team
Ishida, N.; Saitoh, S.; Tokuhiro, K.; Nagamori, E.; Matsuyama, T.; Kitamoto, K.; Takahashi, H.
Efficient production of L-Lactic acid by metabolically engineered Saccharomyces cerevisiae with a genome-integrated L-lactate dehydrogenase gene
Appl. Environ. Microbiol.
71
1964-1970
2005
Bifidobacterium longum, Bifidobacterium longum (P0CW93), Bos taurus
Manually annotated by BRENDA team
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