Sequence of LDH_GEOSE
EC Number:1.1.1.27
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
(S)-lactate + NAD+ = pyruvate + NADH + H+
Other sequences found for EC No. 1.1.1.27
General information:
Sequence
0 MKNNGGARVV VIGAGFVGAS YVFALMNQGI ADEIVLIDAN ESKAIGDAMD FNHGKVFAPK
60 PVDIWHGDYD DCRDADLVVI CAGANQKPGE TRLDLVDKNI AIFRSIVESV MASGFQGLFL
120 VATNPVDILT YATWKFSGLP HERVIGSGTI LDTARFRFLL GEYFSVAPQN VHAYIIGEHG
180 DTELPVWSQA YIGVMPIRKL VESKGEEAQK DLERIFVNVR DAAYQIIEKK GATYYGIAMG
240 LARVTRAILH NENAILTVSA YLDGLYGERD VYIGVPAVIN RNGIREVIEI ELNDDEKNRF
300 HHSAATLKSV LARAFTR
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
947512
Barstow D.A.,Clarke A.R.,Chia W.N.,Wigley D.,Sharman A.F.,Holbrook J.J.,Atkinson T.,Minton N.P.
Cloning, expression and complete nucleotide sequence of the Bacillus stearothermophilus L-lactate dehydrogenase gene.
Gene
46
47-55
1986
947513
Zuelli F.,Weber H.,Zuber H.
Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria, VI. Nucleotide sequences of lactate dehydrogenase genes from the thermophilic bacteria Bacillus stearothermophilus, B. caldolyticus and B. caldotenax.
Biol. Chem. Hoppe-Seyler
368
1167-1177
1987
947514
Tratschin J.D.,Wirz B.,Frank G.,Zuber H.
Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria. II) The primary structure of thermophilic lactate dehydrogenase from Bacillus stearothermophilus. Cyanogen bromide fragments and partial sequence.
Hoppe-Seyler's Z. Physiol. Chem.
364
879-892
1983
947515
Wirz B.,Suter F.,Zuber H.
Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria. III) The primary structure of thermophilic lactate dehydrogenase from Bacillus stearothermophilus. Hydroxylamine-, o-iodosobenzoic acid- and tryptic-fragments. The complete amino-acid sequence.
Hoppe-Seyler's Z. Physiol. Chem.
364
893-909
1983
947517
Clarke A.R.,Wigley D.B.,Barstow D.A.,Chia W.N.,Atkinson T.,Holbrook J.J.
A single amino acid substitution deregulates a bacterial lactate dehydrogenase and stabilizes its tetrameric structure.
Biochim. Biophys. Acta
913
72-80
1987
947518
Piontek K.,Chakrabarti P.,Schar H.P.,Rossmann M.G.,Zuber H.
Structure determination and refinement of Bacillus stearothermophilus lactate dehydrogenase.
Proteins
7
74-92
1990
947519
Wigley D.B.,Gamblin S.J.,Turkenburg J.P.,Dodson E.J.,Piontek K.,Muirhead H.,Holbrook J.J.
Structure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5-A resolution.
J. Mol. Biol.
223
317-335
1992
