PKLR

From Wikipedia, the free encyclopedia

Pyruvate kinase, liver and RBC

PDB rendering based on 1liu.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
2VGB, 2VGF, 2VGG, 2VGI, 4IMA, 4IP7

Identifiers

Symbols

PKLR; PK1; PKL; PKR; PKRL; RPK

External IDs

OMIM: 609712 MGI: 97604 HomoloGene: 37286 ChEMBL: 1075126 GeneCards: PKLR Gene

EC number

2.7.1.40

Gene Ontology
Molecular function	• magnesium ion binding • pyruvate kinase activity • ATP binding • potassium ion binding
Cellular component	• cytosol
Biological process	• response to hypoxia • carbohydrate metabolic process • glucose metabolic process • glycolysis • energy reserve metabolic process • ATP biosynthetic process • response to nutrient • response to heat • response to glucose stimulus • response to lithium ion • endocrine pancreas development • positive regulation of cellular metabolic process • cellular response to insulin stimulus • response to ATP • pyruvate biosynthetic process • small molecule metabolic process • response to cAMP • response to other organism
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
155.26 – 155.27 Mb

Chr 3:
89.14 – 89.15 Mb

PubMed search

Pyruvate kinase isozymes R/L 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 phosphoenolpyruvate from pyruvate and ATP. 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]

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles. ^{[§ 1]}

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Glycolysis and Gluconeogenesis edit

↑ The interactive pathway map can be edited at WikiPathways: "GlycolysisGluconeogenesis_WP534".

References

↑ Tani K, Fujii H, Tsutsumi H, Sukegawa J, Toyoshima K, Yoshida MC, Noguchi T, Tanaka T, Miwa S (Apr 1987). "Human liver type pyruvate kinase: cDNA cloning and chromosomal assignment". Biochem Biophys Res Commun 143 (2): 431–8. doi:10.1016/0006-291X(87)91372-6. PMID 3566732.
↑ 2.0 2.1 "Entrez Gene: PKLR pyruvate kinase, liver and RBC".

Beutler E, Baronciani L (1996). "Mutations in pyruvate kinase.". Hum. Mutat. 7 (1): 1–6. doi:10.1002/(SICI)1098-1004(1996)7:1<1::AID-HUMU1>3.0.CO;2-H. PMID 8664896.
Baronciani L, Bianchi P, Zanella A (1999). "Hematologically important mutations: red cell pyruvate kinase (2nd update).". Blood Cells Mol. Dis. 24 (3): 273–9. doi:10.1006/bcmd.1998.0193. PMID 10087985.
Zanella A, Fermo E, Bianchi P, et al. (2007). "Pyruvate kinase deficiency: the genotype-phenotype association.". Blood Rev. 21 (4): 217–31. doi:10.1016/j.blre.2007.01.001. PMID 17360088.
Kanno H, Fujii H, Miwa S (1992). "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. doi:10.1016/0006-291X(92)91086-6. PMID 1445295.
Kanno H, Fujii H, Hirono A, et al. (1992). "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. PMID 1536957.
Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin.". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
Kanno H, Fujii H, Hirono A, Miwa S (1991). "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. doi:10.1073/pnas.88.18.8218. PMC 52478. PMID 1896471.
Neubauer B, Lakomek M, Winkler H, et al. (1991). "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. PMID 2018831.
Tani K, Fujii H, Nagata S, Miwa S (1988). "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. doi:10.1073/pnas.85.6.1792. PMC 279865. PMID 3126495.
Satoh H, Tani K, Yoshida MC, et al. (1988). "The human liver-type pyruvate kinase (PKL) gene is on chromosome 1 at band q21.". Cytogenet. Cell Genet. 47 (3): 132–3. doi:10.1159/000132530. PMID 3378452.
Baronciani L, Beutler E (1995). "Molecular study of pyruvate kinase deficient patients with hereditary nonspherocytic hemolytic anemia.". J. Clin. Invest. 95 (4): 1702–9. doi:10.1172/JCI117846. PMC 295683. PMID 7706479.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Kanno H, Ballas SK, Miwa S, et al. (1994). "Molecular abnormality of erythrocyte pyruvate kinase deficiency in the Amish.". Blood 83 (8): 2311–6. PMID 8161798.
Lenzner C, Nürnberg P, Thiele BJ, et al. (1994). "Mutations in the pyruvate kinase L gene in patients with hereditary hemolytic anemia.". Blood 83 (10): 2817–22. PMID 8180378.
Kanno H, Fujii H, Tsujino G, Miwa S (1993). "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. doi:10.1006/bbrc.1993.1379. PMID 8476433.
Kanno H, Fujii H, Miwa S (1993). "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. PMID 8481523.
Baronciani L, Beutler E (1993). "Analysis of pyruvate kinase-deficiency mutations that produce nonspherocytic hemolytic anemia.". Proc. Natl. Acad. Sci. U.S.A. 90 (9): 4324–7. doi:10.1073/pnas.90.9.4324. PMC 46499. PMID 8483951.
Baronciani L, Bianchi P, Zanella A (1996). "Hematologically important mutations: red cell pyruvate kinase.". Blood Cells Mol. Dis. 22 (1): 85–9. doi:10.1006/bcmd.1996.0012. PMID 8807089.

PDB gallery

1liu:

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Metabolism: carbohydrate metabolism: glycolysis/gluconeogenesis enzymes

Glycolysis

Gluconeogenesis only

to oxaloacetate:	Pyruvate carboxylase Phosphoenolpyruvate carboxykinase

from lactate (Cori cycle):	Lactate dehydrogenase

from alanine (Alanine cycle):	Alanine transaminase

from glycerol:	Glycerol kinase Glycerol dehydrogenase

Regulatory

M: MET

mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m

k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon

m (A16/C10), i (k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)

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PKLR

Interactive pathway map

See also

References

Further reading