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Sequence of LDH_PRIMG

EC Number:1.1.1.27

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
L-lactate dehydrogenase
P00345
Priestia megaterium
318
35035
Reaction
(S)-lactate + NAD+ = pyruvate + NADH + H+
Other sequences found for EC No. 1.1.1.27

General information:

Sequence
show sequence in fasta format
  0 MKTQFTPKTR KVAVIGTGFV GSSYAFSMVN QGIANELVLI DMNKEKAEGE ARDINHGMPF
 60 ATPMKIWAGD YKDCADADLA VITAGANQAP GETRLDLVEK NVKIFECIVK DIMNSGFDGI
120 ILVATNPVDI LAHVTQKVSG LPNGRVIGSG TILDTARFRY LLSDYFEVDS RNVHAYIMGE
180 HGDTEFPVWS HAQIGGVKLE HFINTAAIEK EPDMQHLFEQ TRDAAYHIIN RKGATYYGIA
240 MGLVRITKAI LDDENSILTV SALLEGQYGI SDVYIGVPAI INKNGVRQII ELNLTPHEQQ
300 QLEHSASILK QTRDRAFV
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1078252
Waldvogel S.,Weber H.,Zuber H.
Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria. VII. Nucleotide sequence of the lactate dehydrogenase gene from the mesophilic bacterium Bacillus megaterium. Preparation and properties of a hybrid lactate dehydrogenase comprising moieties of the B. megaterium and B. stearothermophilus enzymes.
Biol. Chem. Hoppe-Seyler
368
1391-1399
1987
1078253
Stangl D.,Wiederkehr F.,Suter F.,Zuber H.
Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria, V. The complete amino-acid sequence of the mesophilic L-lactate dehydrogenase from Bacillus megaterium.
Biol. Chem. Hoppe-Seyler
368
1157-1166
1987