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The complete primary structure of the allosteric L-lactate dehydrogenase from Lactobacillus casei.
The polypeptide chain of the allosteric L-lactate dehydrogenase (EC 1.1.1.27) of Lactobacillus casei consists of 325 amino acid residues. Despite the strikingly different enzymatic characteristics of the allosteric L-lactate dehydrogenase of L. casei and of the non-allosteric vertebrate enzymes, the sequence of the allosteric enzyme shows a distinct homology with that of the non-allosteric vertebrate enzymes (average identity: 37%). An especially high sequence homology can be identified within the active center (average identity: 70%). A clear deviation of the L. casei enzyme from the vertebrate enzyme is the lack of the first 12 amino acid residues at the N terminus and an additional 7 amino acid residues at the C terminus. The localization of the binding site of the allosteric effector D-fructose 1,6-bisphosphate and pH and effector-induced changes of the spectroscopic properties are discussed on the basis of the primary structure.
PMID: 6411465 [PubMed - indexed for MEDLINE]
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Cited by 6 PubMed Central articles
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Lactate dehydrogenase from Streptococcus mutans: purification, characterization, and crossed antigenicity with lactate dehydrogenases from Lactobacillus casei, Actinomyces viscosus, and Streptococcus sanguis.
Sommer P, Klein JP, Schöller M, Frank RM.
Infect Immun. 1985 Feb; 47(2):489-95.
[Infect Immun. 1985]
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Immunological study of lactate dehydrogenase from Streptococcus mutans and evidence of common antigenic domains with lactate dehydrogenases from lactic bacteria.
Sommer P, Klein JP, Ogier JA, Frank RM.
Infect Immun. 1986 Jan; 51(1):277-81.
[Infect Immun. 1986]
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DNA sequence and in vitro mutagenesis of the gene encoding the fructose-1,6-diphosphate-dependent L-(+)-lactate dehydrogenase of Streptococcus mutans.
Duncan MJ, Hillman JD.
Infect Immun. 1991 Nov; 59(11):3930-4.
[Infect Immun. 1991]
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Structures reported by this article