Structural Constraints of Possible Mechanisms of Lactate Dehydrogenase as Shown by High Resolution Studies of the Apoenzyme and a Variety of Enzyme Complexes

Rossmann, M.G.; Adams, Margaret; Buehner, Manfred; Ford, Geoffrey C.; Hackert, Marvin L.; Lentz, P. J.; McPherson, Alexander; Schevitz, Richard W.; Smiley, Ira E.

doi:10.1101/sqb.1972.036.01.025

Cited by 99 publications

(34 citation statements)

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“…Long segments of possible but distant homology are found between GPDH and LADH (11) or GDH (12). Similarities in the tertiary structures of LDH (13), soluble malate dehydrogenase (14), LADH (15), and GPDH (16) are also evident. Ancestral connections between different dehydrogenases are therefore likely, although evolutionary relationships are not clear.…”

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confidence: 74%

“…The available structure of YADH was therefore systematically searched for identities with LADH (28), GPDH. (10), and known segments of LDH (13,29), by the diagram method (30), in which "diagonal matching" indicates similarities.…”

Section: Structure Of Yadh Compared With Other Dehydrogenasesmentioning

confidence: 99%

“…Thus, both YADH and LADH have alcohol as substrate and contain zinc (17,18), in contrast to LDH (13) and GPDH (19). On the other hand, YADH, LDH, and GPDH are all tetrameric with subunits of molecular weight about 36,000 (7,13,20), whereas LADH is dimeric with subunits of molecular weight 40,000 (21).…”

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confidence: 99%

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Partial Similarities Between Yeast and Liver Alcohol Dehydrogenases

Jörnvall

1973

Proc. Natl. Acad. Sci. U.S.A.

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The primary structure of about half of the protein chain of yeast alcohol dehydrogenase has been determined and compared with the amino-acid sequences of other dehydrogenases. The enzyme is found to be distantly related to horse-liver alcohol dehydrogenase, although these two proteins have different quaternary structures and subunit sizes. Some regions show no significant similarities, but long segments within the N-terminal parts of the molecules are homologous, suggesting a common and important function for these segments. Ancestral connections between some different dehydrogenases can be concluded and the degree of evolutionary changes may be estimated.

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confidence: 74%

Section: Structure Of Yadh Compared With Other Dehydrogenasesmentioning

confidence: 99%

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Partial Similarities Between Yeast and Liver Alcohol Dehydrogenases

Jörnvall

1973

Proc. Natl. Acad. Sci. U.S.A.

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“…Such analyses have shown that protein motion may occur due to conformational changes in individual residues or at the secondary, tertiary, or quaternary structural levels. Lactate dehydrogenase, 2,3 triose-phosphate isomerase, 4 as well as hemoglobin and related proteins 5 are some of the earliest examples of proteins that showed conformational changes with important functional implications. Subsequent analyses of different protein families have identified common structural domains 6 that undergo functionally relevant conformational changes.…”

Section: Introductionmentioning

confidence: 99%

Control of protein functional dynamics by peptide linkers

2005

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Control of structural flexibility is essential for the proper functioning of a large number of proteins and multiprotein complexes. At the residue level, such flexibility occurs due to local relaxation of peptide bond angles whose cumulative effect may result in large changes in the secondary, tertiary or quaternary structures of protein molecules. Such flexibility, and its absence, most often depends on the nature of interdomain linkages formed by oligopeptides. Both flexible and relatively rigid peptide linkers are found in many multidomain proteins. Linkers are thought to control favorable and unfavorable interactions between adjacent domains by means of variable softness furnished by their primary sequence. Large-scale structural heterogeneity of multidomain proteins and their complexes, facilitated by soft peptide linkers, is now seen as the norm rather than the exception. Biophysical discoveries as well as computational algorithms and databases have reshaped our understanding of the often spectacular biomolecular dynamics enabled by soft linkers. Absence of such motion, as in so-called molecular rulers, also has desirable functional effects in protein architecture. We review here the historic discovery and current understanding of the nature of domains and their linkers from a structural, computational, and biophysical point of view. A number of emerging applications, based on the current understanding of the structural properties

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“…The structural analysis of lactate dehydrogenase [1], malate dehydrogenase [2], liver alcohol dehydrogenase [3], and glyceraldehyde 3-phosphate dehydrogenase [4] show striking homologies within this group of proteins, particularly of the NAD-binding sites. However, no detailed structural information is available on a class of enzymes using NADP, of which 6-phosphogluconate dehydrogenase (6PGD) is a member.…”

Section: Introductionmentioning

confidence: 99%