Lactate dehydrogenase A

M5. Maekawa, M Sudo, K., Kanno, T., and Li, S. S.-L., Molecular characterization of genetic mutation in human lactate dehydrogenase-A (M) deficiency. Biochem. Biophys. Res. Commun. 168, 677-682 (1990). 

RGURE 13-16 The nucleotide binding domain of the enzyme lactate dehydrogenase, (a) The Rossmann fold is a structural motif found in the NAD-binding site of many dehydrogenases It consists of a six-stranded parallel /3 sheet and four a helices inspection reveals the arrangement to be a pair of structurally similar motifs... 

Firth, J.D., B.L. Ebert, C.W. Pugh, andP.J. Ratcliffe (1994). Oxygen-regulated control elements in the phosphoglycerate kinase 1 and lactate dehydrogenase A genes Similarities with the erythropoietin 3 enhancer. Proc. Natl. Acad. Sci. USA 91 6496-6500. 

Firth, J.D., B.L. Ebert and P.J. Ratcliffe (1995). Hypoxic regulation of lactate dehydrogenase A. Interaction between hypoxia inducible factor 1 and cAMP response elements. J. Biol. Chem. 270 21021-21027. 

Semenza, G.L., B. Jiang, S.W. Leung, R. Passantino, J. Concordet, P. Maire, and A. Giallongo (1996). Hypoxia response elements in the aldolase A, eno-lase 1, and lactate dehydrogenase A gene promoters contain essential binding sites for hypoxia Inducible Factor-1. J. Biol. Chem. 271 32529-32537. 

Lactate dehydrogenase a model enzyme for studying adaptation to temperature... 

Holland, L.Z., M. McFall-Ngai, and G.N. Somero (1997). Evolution of lactate dehydrogenase-A homologs of barracuda fishes (genus Sphyraena) from different thermal environments Differences in kinetic properties and thermal stability are due to amino acid substitutions outside the active site. Biochemistry 36 3207-3215. 

Hols, P., Ramos, A., Hugenholtz, J., Delcour, I, De Vos, W. M., Santos, H., and Kleerebezem, M. 1999. Acetate utilization in Lactococcus lactis deficient in lactate dehydrogenase A rescue pathway for maintaining redox balance. J. Bacteriol., 181, 5521-5526. 

Fig. 19. The active sites of lactate dehydrogenase (A) and glyceraldehyde-3-phosphate dehydrogenase (B). From the work of Rossmann and colleagues [52],...

Deng, H., Zheng, J., Burgner, J., and Callender, R., Molecular properties of pyruvate bound to lactate dehydrogenase A Raman spectroscopic study, Proc. Nat. Acad. Sci., USA 86, 4484-4488 (1989). 

Figure 10.27. Isozymes of Lactate Dehydrogenase. (A) The rat heart LDH isozyme profile changes in the course of development. The H isozyme is represented by squares and the M isozyme by circles. The negative and positive numbers denote the days before and after birth, respectively. (B) LDH isozyme content varies by tissue. [(A) After W.-H. Li, Molecular Evolution (Sinauer, 1997), p. 283 (B) After K. Urich, Comparative Animal Biochemistry (S nngQrVQrlag, 1990), p. 542.]...

Resistance to vancomycin is via a sensor histidine kinase (VanS) and a response regulator (VanR). VanH encodes a D-lactate dehydrogenase/a-keto acid reductase and generates D-lactate, which is the substrate for VanA, a D-Ala-D-Lac ligase. The result is cell wall precursors terminating in D-Ala-D-... 

Certain gene loci may be expressed almost exclusively in a single tissue, perhaps at a particular stage in development. In addition to the two gene loci that determine the two most common subunits of lactate dehydrogenase, a third locus is active only in mature testes. It determines the structure of a third type of subunit, X or C, which makes up a specific isoenzyme, LD-X or LD-C, found only in testes. The isoenzyme of ALP that occurs in the human placenta is the product of a single structural gene locus, which is distinct from the loci that specify the structures of other forms of ALP, and the product of the placental phosphatase locus is normally detectable only in the placenta. 

Figure 22.5 An example of reactions involved in an enzyme-catalyzed recycling processes for amplification of the sensitivity. In the left part (A) of the figure the enzyme-pair hexokinase and pyruvate kinase is used for recycling of the coenzyme ATP/ADP. In the right part (B), substrate recycling of pymvate or lactate is accomplished using the enzyme-pair lactate oxidase/lactate dehydrogenase. A multiplication effect is obtained by combination of A and B resulting in a very high sensitivity [27], The calorimetric sensitivity is further inreased by including catalase (cat).

A profile of the serum isoenzymes of lactate dehydrogenase, (a) The pattern of LDH isoenzymes from a normal individual, (b) The pattern of LDH isoenzymes of an individual suffering from a myocardial infarction. 

Ream R., Johns G., Somero G. (2003). Base compositions of genes encoding a-actin and lactate dehydrogenase-A from differently adapted vertebrates show no temperature-adaptive variation in G+C content. Mol. Biol. Evol. 20 105-110. 

Fig. 2 Lactate dehydrogenase a) a ribbon representation of the tetramer of the B. stearothermophilus enzyme with each peptide chain depicted in a different color. The cofactor and oxamate inhibitor are colored according to atom type, as is fructose bisphosphate. which is an allosteric regulator of the enzyme, b) On the left is a detailed view of the enzyme active site as seen in the crystal structure. The ligand is highlighted in green and key amino acid residues are labeled. This is compared with the traditional two-dimensional representation of the enzyme mechanism on the right. Note that the residue numbers differ slightly from those of the muscle enzyme discussed in the test. (View this an i i color at www.dekker.com.)...

RA Pearson, S Tart, J Tucker, J.A., Vogtherr, M Whittaker, D Wingfield, J Winter, J and Hudson, K. (2012) Design and synthesis of novel lactate dehydrogenase A inhibitors by fragment-based lead generation. Journal of Medicinal Chemistry, 55 3285-3306. 

Matusiewiez SP, Williamson IJ, Sime PJ, et al. Plasma lactate dehydrogenase. A marker of disease activity in cr)fptogenic fibrosing alveolitis and extrinsic allergic alveolitis. Eur Respir J 1993 6(9) 1282-1286. 

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