LDHA
Lactate dehydrogenase A, also known as LDHA, is an enzyme which in humans is encoded by the LDHA gene.[1]
Function
Lactate dehydrogenase A catalyzes the conversion of L-lactate and NAD+ to pyruvate and NADH in the final step of anaerobic glycolysis. LDHA is found predominantly in muscle tissue and belongs to the lactate dehydrogenase family. Mutations in LDHA have been linked to exertional myoglobinuria.[2]
References
Further reading
- Miyajima H, Shimizu T, Kaneko E (1993). "[Gene expression in lactate dehydrogenase-A subunit deficiency]". Rinsho Shinkeigaku 32 (10): 1087–92. PMID 1297552.
- Sudo K, Maekawa M, Shioya M et al. (1992). "Molecular analysis of genetic mutation in electrophoretic variant of human lactate dehydrogenase-A(M) subunit". Biochem. Int. 27 (6): 1051–7. PMID 1445373.
- Maekawa M, Sudo K, Li SS, Kanno T (1991). "Analysis of genetic mutations in human lactate dehydrogenase-A(M) deficiency using DNA conformation polymorphism in combination with polyacrylamide gradient gel and silver staining". Biochem. Biophys. Res. Commun. 180 (2): 1083–1090. doi:10.1016/S0006-291X(05)81177-5. PMID 1953713.
- Maekawa M, Sudo K, Li SS, Kanno T (1992). "Genotypic analysis of families with lactate dehydrogenase A (M) deficiency by selective DNA amplification". Hum. Genet. 88 (1): 34–38. doi:10.1007/BF00204925. PMID 1959923.
- Scrable HJ, Johnson DK, Rinchik EM, Cavenee WK (1990). "Rhabdomyosarcoma-associated locus and MYOD1 are syntenic but separate loci on the short arm of human chromosome 11". Proc. Natl. Acad. Sci. U.S.A. 87 (6): 2182–2186. doi:10.1073/pnas.87.6.2182. PMC 53650. PMID 2315312. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=53650.
- Maekawa M, Sudo K, Kanno T, Li SS (1990). "Molecular characterization of genetic mutation in human lactate dehydrogenase-A (M) deficiency". Biochem. Biophys. Res. Commun. 168 (2): 677–682. doi:10.1016/0006-291X(90)92374-9. PMID 2334430.
- Gosti F, Marty MC, Courvalin JC et al. (1987). "Centrosomal proteins and lactate dehydrogenase possess a common epitope in human cell lines". Proc. Natl. Acad. Sci. U.S.A. 84 (4): 1000–1004. doi:10.1073/pnas.84.4.1000. PMC 304349. PMID 2434947. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=304349.
- Chung FZ, Tsujibo H, Bhattacharyya U et al. (1986). "Genomic organization of human lactate dehydrogenase-A gene". Biochem. J. 231 (3): 537–41. PMC 1152784. PMID 3000353. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1152784.
- Tsujibo H, Tiano HF, Li SS (1985). "Nucleotide sequences of the cDNA and an intronless pseudogene for human lactate dehydrogenase-A isozyme". Eur. J. Biochem. 147 (1): 9–15. doi:10.1111/j.1432-1033.1985.tb08711.x. PMID 3838278.
- Glass RD, Doyle D (1972). "Genetic control of lactate dehydrogenase expression in mammalian tissues". Science 176 (4031): 180–181. doi:10.1126/science.176.4031.180. PMID 5014440.
- Maekawa M, Sudo K, Kobayashi A et al. (1994). "Fast-type electrophoretic variant of lactate dehydrogenase M(A) and comparison with other missense mutations in lactate dehydrogenase M(A) and H(B) genes". Clin. Chem. 40 (4): 665–8. PMID 7908613.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–174. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Miyajima H, Takahashi Y, Suzuki M et al. (1993). "Molecular characterization of gene expression in human lactate dehydrogenase-A deficiency". Neurology 43 (7): 1414–9. PMID 8327147.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–156. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Scanlan MJ, Gordan JD, Williamson B et al. (1999). "Antigens recognized by autologous antibody in patients with renal-cell carcinoma". Int. J. Cancer 83 (4): 456–464. doi:10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5. PMID 10508479.
- Vilà MR, Nicolás A, Morote J et al. (2000). "Increased glyceraldehyde-3-phosphate dehydrogenase expression in renal cell carcinoma identified by RNA-based, arbitrarily primed polymerase chain reaction". Cancer 89 (1): 152–164. doi:10.1002/1097-0142(20000701)89:1<152::AID-CNCR20>3.0.CO;2-T. PMID 10897012.
- Boutet A, Altmeyer R, Héry C, Tardieu M (2001). "Direct role of plasma membrane-expressed gp120/41 in toxicity to human astrocytes induced by HIV-1-infected macrophages". AIDS 14 (17): 2687–2697. doi:10.1097/00002030-200012010-00008. PMID 11125887.
- Read JA, Winter VJ, Eszes CM et al. (2001). "Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase". Proteins 43 (2): 175–185. doi:10.1002/1097-0134(20010501)43:2<175::AID-PROT1029>3.0.CO;2-#. PMID 11276087.
- Sung JH, Shin SA, Park HK et al. (2001). "Protective effect of glutathione in HIV-1 lytic peptide 1-induced cell death in human neuronal cells". J. Neurovirol. 7 (5): 454–465. doi:10.1080/135502801753170318. PMID 11582518.
- Pioli PA, Hamilton BJ, Connolly JE et al. (2002). "Lactate dehydrogenase is an AU-rich element-binding protein that directly interacts with AUF1". J. Biol. Chem. 277 (38): 35738–35745. doi:10.1074/jbc.M204002200. PMID 12107167.
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PDB gallery
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1i10: HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE
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9ldb: DESIGN AND SYNTHESIS OF NEW ENZYMES BASED ON THE LACTATE DEHYDROGENASE FRAMEWORK
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9ldt: DESIGN AND SYNTHESIS OF NEW ENZYMES BASED ON THE LACTATE DEHYDROGENASE FRAMEWORK
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