Open AccessAminoacid Sequence of Dogfish M 4 Lactate Dehydrogenase
Author(s) -
Susan S. Taylor,
Susanna S. Oxley,
William S. Allison,
Nathan O. Kaplan
Publication year - 1973
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.70.6.1790
Subject(s) - lactate dehydrogenase , dehydrogenase , biochemistry , alcohol dehydrogenase , histidine , peptide sequence , biology , branched chain alpha keto acid dehydrogenase complex , cysteine , enzyme , chemistry , microbiology and biotechnology , gene
About 80% of the aminoacid sequence of dogfish (Squalus acanthius) M(4) lactate dehydrogenase (EC 1.1.1.27) has been elucidated. Several sequence homologies with peptides from pig H(4) and pig M(4) lactate dehydrogenase are identified. Histidine 195 is homologous to the essential histidine residue in pig H(4) lactate dehydrogenase. Similarities in the sequence around the "essential" cysteine residue of lactate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, and yeast and liver alcohol dehydrogenase are delineated.
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