Sequence of DLDH_PEA
EC Number:1.8.1.4
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
Other sequences found for EC No. 1.8.1.4
General information:
Sequence
0 MAMANLARRK GYSLLSSETL RYSFSLRSRA FASGSDENDV VIIGGGPGGY VAAIKAAQLG
60 FKTTCIEKRG ALGGTCLNVG CIPSKALLHS SHMYHEAKHS FANHGVKVSN VEIDLAAMMG
120 QKDKAVSNLT RGIEGLFKKN KVTYVKGYGK FVSPSEISVD TIEGENTVVK GKHIIIATGS
180 DVKSLPGVTI DEKKIVSSTG ALALSEIPKK LVVIGAGYIG LEMGSVWGRI GSEVTVVEFA
240 SEIVPTMDAE IRKQFQRSLE KQGMKFKLKT KVVGVDTSGD GVKLTVEPSA GGEQTIIEAD
300 VVLVSAGRTP FTSGLNLDKI GVETDKLGRI LVNERFSTNV SGVYAIGDVI PGPMLAHKAE
360 EDGVACVEYL AGKVGHVDYD KVPGVVYTNP EVASVGKTEE QVKETGVEYR VGKFPFMANS
420 RAKAIDNAEG LVKIIAEKET DKILGVHIMA PNAGELIHEA AIALQYDASS EDIARVCHAH
480 PTMSEAIKEA AMATYDKPIH I
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
153257
Bourguignon J.,Macherel D.,Neuburger M.,Douce R.
Isolation, characterization, and sequence analysis of a cDNA clone encoding L-protein, the dihydrolipoamide dehydrogenase component of the glycine cleavage system from pea-leaf mitochondria.
Eur. J. Biochem.
204
865-873
1992
153259
Turner S.R.,Ireland R.,Rawsthorne S.
Purification and primary amino acid sequence of the L subunit of glycine decarboxylase. Evidence for a single lipoamide dehydrogenase in plant mitochondria.
J. Biol. Chem.
267
7745-7750
1992
153261
Bourguignon J.,Merand V.,Rawsthorne S.,Forest E.,Douce R.
Glycine decarboxylase and pyruvate dehydrogenase complexes share the same dihydrolipoamide dehydrogenase in pea leaf mitochondria: evidence from mass spectrometry and primary-structure analysis.
Biochem. J.
313
229-234
1996
153262
Faure M.,Bourguignon J.,Neuburger M.,MacHerel D.,Sieker L.,Ober R.,Kahn R.,Cohen-Addad C.,Douce R.
Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system 2. Crystal structures of H- and L-proteins.
Eur. J. Biochem.
267
2890-2898
2000
