Pyruvate kinase PKLR explained

Pyruvate kinase PKLR is an enzyme that in humans is encoded by the PKLR gene.^{[1] [2]}

The protein encoded by this gene is a pyruvate kinase that catalyzes the production of pyruvate and ATP from phosphoenolpyruvate. Defects in this enzyme, due to gene mutations or genetic variations, are the common cause of chronic hereditary nonspherocytic hemolytic anemia (CNSHA or HNSHA). Alternatively spliced transcript variants encoding distinct isoforms have been described.^[2]

Further reading

• Beutler E, Baronciani L . Mutations in pyruvate kinase. . Hum. Mutat. . 7 . 1 . 1–6 . 1996 . 8664896 . 10.1002/(SICI)1098-1004(1996)7:1<1::AID-HUMU1>3.0.CO;2-H . 2481467 . free .
• Baronciani L, Bianchi P, Zanella A . Hematologically important mutations: red cell pyruvate kinase (2nd update). . Blood Cells Mol. Dis. . 24 . 3 . 273–9 . 1999 . 10087985 . 10.1006/bcmd.1998.0193 .
• Zanella A, Fermo E, Bianchi P, etal . Pyruvate kinase deficiency: the genotype-phenotype association. . Blood Rev. . 21 . 4 . 217–31 . 2007 . 17360088 . 10.1016/j.blre.2007.01.001 .
• Kanno H, Fujii H, Miwa S . Structural analysis of human pyruvate kinase L-gene and identification of the promoter activity in erythroid cells. . Biochem. Biophys. Res. Commun. . 188 . 2 . 516–23 . 1992 . 1445295 . 10.1016/0006-291X(92)91086-6 .
• Kanno H, Fujii H, Hirono A, etal . Identical point mutations of the R-type pyruvate kinase (PK) cDNA found in unrelated PK variants associated with hereditary hemolytic anemia. . Blood . 79 . 5 . 1347–50 . 1992 . 10.1182/blood.V79.5.1347.1347 . 1536957 . free .
• Dawson SJ, White LA . Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. . J. Infect. . 24 . 3 . 317–20 . 1992 . 1602151 . 10.1016/S0163-4453(05)80037-4 .
• Kanno H, Fujii H, Hirono A, Miwa S . cDNA cloning of human R-type pyruvate kinase and identification of a single amino acid substitution (Thr384----Met) affecting enzymatic stability in a pyruvate kinase variant (PK Tokyo) associated with hereditary hemolytic anemia. . Proc. Natl. Acad. Sci. U.S.A. . 88 . 18 . 8218–21 . 1991 . 1896471 . 10.1073/pnas.88.18.8218 . 52478 . 1991PNAS...88.8218K . free .
• Neubauer B, Lakomek M, Winkler H, etal . Point mutations in the L-type pyruvate kinase gene of two children with hemolytic anemia caused by pyruvate kinase deficiency. . Blood . 77 . 9 . 1871–5 . 1991 . 10.1182/blood.V77.9.1871.1871 . 2018831 . free .
• Tani K, Fujii H, Nagata S, Miwa S . Human liver type pyruvate kinase: complete amino acid sequence and the expression in mammalian cells. . Proc. Natl. Acad. Sci. U.S.A. . 85 . 6 . 1792–5 . 1988 . 3126495 . 10.1073/pnas.85.6.1792 . 279865 . 1988PNAS...85.1792T . free .
• Satoh H, Tani K, Yoshida MC, etal . The human liver-type pyruvate kinase (PKL) gene is on chromosome 1 at band q21. . Cytogenet. Cell Genet. . 47 . 3 . 132–3 . 1988 . 3378452 . 10.1159/000132530 .
• Baronciani L, Beutler E . Molecular study of pyruvate kinase deficient patients with hereditary nonspherocytic hemolytic anemia. . J. Clin. Invest. . 95 . 4 . 1702–9 . 1995 . 7706479 . 10.1172/JCI117846 . 295683 .
• Maruyama K, Sugano S . Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. . Gene . 138 . 1–2 . 171–4 . 1994 . 8125298 . 10.1016/0378-1119(94)90802-8 .
• Kanno H, Ballas SK, Miwa S, etal . Molecular abnormality of erythrocyte pyruvate kinase deficiency in the Amish. . Blood . 83 . 8 . 2311–6 . 1994 . 10.1182/blood.V83.8.2311.2311 . 8161798 . free .
• Lenzner C, Nürnberg P, Thiele BJ, etal . Mutations in the pyruvate kinase L gene in patients with hereditary hemolytic anemia. . Blood . 83 . 10 . 2817–22 . 1994 . 10.1182/blood.V83.10.2817.2817 . 8180378 . free .
• Kanno H, Fujii H, Tsujino G, Miwa S . Molecular basis of impaired pyruvate kinase isozyme conversion in erythroid cells: a single amino acid substitution near the active site and decreased mRNA content of the R-type PK. . Biochem. Biophys. Res. Commun. . 192 . 1 . 46–52 . 1993 . 8476433 . 10.1006/bbrc.1993.1379 .
• Kanno H, Fujii H, Miwa S . Low substrate affinity of pyruvate kinase variant (PK Sapporo) caused by a single amino acid substitution (426 Arg-->Gln) associated with hereditary hemolytic anemia. . Blood . 81 . 9 . 2439–41 . 1993 . 10.1182/blood.V81.9.2439.bloodjournal8192439 . 8481523 . free .
• Baronciani L, Beutler E . Analysis of pyruvate kinase-deficiency mutations that produce nonspherocytic hemolytic anemia. . Proc. Natl. Acad. Sci. U.S.A. . 90 . 9 . 4324–7 . 1993 . 8483951 . 10.1073/pnas.90.9.4324 . 46499 . 1993PNAS...90.4324B . free .
• Baronciani L, Bianchi P, Zanella A . Hematologically important mutations: red cell pyruvate kinase. . Blood Cells Mol. Dis. . 22 . 1 . 85–9 . 1996 . 8807089 . 10.1006/bcmd.1996.0012 .

Notes and References

1. Web site: PKLR - Pyruvate kinase PKLR - Homo sapiens (Human) - PKLR gene & protein . www.uniprot.org . 26 March 2022 . en.
2. Web site: Entrez Gene: PKLR pyruvate kinase, liver and RBC.