Aldolase B

Aldolase B

Aldolase B is an isoenzyme of fructose 1,6-bisphosphate aldolase (aldolase A), which is also capable of cleaving fructose 1-phosphate to form glyceraldehyde and dihydroxyacetone phosphate (DHAP). The reaction is reversible. Also known as Aldolase (Class II), it is found in the liver and kidney.

Aldolase B, fructose-bisphosphate, also known as ALDOB, is a human gene.cite web | title = Entrez Gene: ALDOB aldolase B, fructose-bisphosphate| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=229| accessdate = ]

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summary_text = Fructose-1,6-bisphosphate aldolase (EC 4.1.2.13 ) is a tetrameric glycolytic enzyme that catalyzes the reversible conversion of fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. Vertebrates have 3 aldolase isozymes which are distinguished by their electrophoretic and catalytic properties. Differences indicate that aldolases A, B, and C are distinct proteins, the products of a family of related 'housekeeping' genes exhibiting developmentally regulated expression of the different isozymes. The developing embryo produces aldolase A, which is produced in even greater amounts in adult muscle where it can be as much as 5% of total cellular protein. In adult liver, kidney and intestine, aldolase A expression is repressed and aldolase B is produced. In brain and other nervous tissue, aldolase A and C are expressed about equally. There is a high degree of homology between aldolase A and C. Defects in ALDOB cause hereditary fructose intolerance.cite web | title = Entrez Gene: ALDOB aldolase B, fructose-bisphosphate| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=229| accessdate = ]

Pathology

Defects of aldolase B cause fructose 1-phosphate to accumulate in tissues which contain fructokinase, a condition known as hereditary fructose intolerance.

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Tolan DR |title=Molecular basis of hereditary fructose intolerance: mutations and polymorphisms in the human aldolase B gene. |journal=Hum. Mutat. |volume=6 |issue= 3 |pages= 210–8 |year= 1996 |pmid= 8535439 |doi= 10.1002/humu.1380060303
*cite journal | author=Cross NC, de Franchis R, Sebastio G, "et al." |title=Molecular analysis of aldolase B genes in hereditary fructose intolerance. |journal=Lancet |volume=335 |issue= 8685 |pages= 306–9 |year= 1990 |pmid= 1967768 |doi=
*cite journal | author=Cross NC, Stojanov LM, Cox TM |title=A new aldolase B variant, N334K, is a common cause of hereditary fructose intolerance in Yugoslavia. |journal=Nucleic Acids Res. |volume=18 |issue= 7 |pages= 1925 |year= 1990 |pmid= 2336380 |doi=
*cite journal | author=Sakakibara M, Mukai T, Yatsuki H, Hori K |title=Human aldolase isozyme gene: the structure of multispecies aldolase B mRNAs. |journal=Nucleic Acids Res. |volume=13 |issue= 14 |pages= 5055–69 |year= 1985 |pmid= 2410860 |doi=
*cite journal | author=Sakakibara M, Takahashi I, Takasaki Y, "et al." |title=Construction and expression of human aldolase A and B expression plasmids in Escherichia coli host. |journal=Biochim. Biophys. Acta |volume=1007 |issue= 3 |pages= 334–42 |year= 1989 |pmid= 2649152 |doi=
*cite journal | author=Mukai T, Yatsuki H, Arai Y, "et al." |title=Human aldolase B gene: characterization of the genomic aldolase B gene and analysis of sequences required for multiple polyadenylations. |journal=J. Biochem. |volume=102 |issue= 5 |pages= 1043–51 |year= 1988 |pmid= 2830249 |doi=
*cite journal | author=Henry I, Gallano P, Besmond C, "et al." |title=The structural gene for aldolase B (ALDB) maps to 9q13----32. |journal=Ann. Hum. Genet. |volume=49 |issue= Pt 3 |pages= 173–80 |year= 1986 |pmid= 3000275 |doi=
*cite journal | author=Tolan DR, Penhoet EE |title=Characterization of the human aldolase B gene. |journal=Mol. Biol. Med. |volume=3 |issue= 3 |pages= 245–64 |year= 1986 |pmid= 3016456 |doi=
*cite journal | author=Cross NC, Tolan DR, Cox TM |title=Catalytic deficiency of human aldolase B in hereditary fructose intolerance caused by a common missense mutation. |journal=Cell |volume=53 |issue= 6 |pages= 881–5 |year= 1988 |pmid= 3383242 |doi=
*cite journal | author=Paolella G, Santamaria R, Izzo P, "et al." |title=Isolation and nucleotide sequence of a full-length cDNA coding for aldolase B from human liver. |journal=Nucleic Acids Res. |volume=12 |issue= 19 |pages= 7401–10 |year= 1984 |pmid= 6548561 |doi=
*cite journal | author=Rottmann WH, Tolan DR, Penhoet EE |title=Complete amino acid sequence for human aldolase B derived from cDNA and genomic clones. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=81 |issue= 9 |pages= 2738–42 |year= 1984 |pmid= 6585824 |doi=
*cite journal | author=Besmond C, Dreyfus JC, Gregori C, "et al." |title=Nucleotide sequence of a cDNA clone for human aldolase B. |journal=Biochem. Biophys. Res. Commun. |volume=117 |issue= 2 |pages= 601–9 |year= 1984 |pmid= 6689266 |doi=
*cite journal | author=Ali M, Cox TM |title=Diverse mutations in the aldolase B gene that underlie the prevalence of hereditary fructose intolerance. |journal=Am. J. Hum. Genet. |volume=56 |issue= 4 |pages= 1002–5 |year= 1995 |pmid= 7717389 |doi=
*cite journal | author=Ali M, Sebastio G, Cox TM |title=Identification of a novel mutation (Leu 256-->Pro) in the human aldolase B gene associated with hereditary fructose intolerance. |journal=Hum. Mol. Genet. |volume=3 |issue= 1 |pages= 203–4 |year= 1994 |pmid= 8162030 |doi=
*cite journal | author=Brooks CC, Tolan DR |title=A partially active mutant aldolase B from a patient with hereditary fructose intolerance. |journal=FASEB J. |volume=8 |issue= 1 |pages= 107–13 |year= 1994 |pmid= 8299883 |doi=
*cite journal | author=Kusakabe T, Motoki K, Hori K |title=Mode of interactions of human aldolase isozymes with cytoskeletons. |journal=Arch. Biochem. Biophys. |volume=344 |issue= 1 |pages= 184–93 |year= 1997 |pmid= 9244396 |doi= 10.1006/abbi.1997.0204
*cite journal | author=Lau J, Tolan DR |title=Screening for hereditary fructose intolerance mutations by reverse dot-blot. |journal=Mol. Cell. Probes |volume=13 |issue= 1 |pages= 35–40 |year= 1999 |pmid= 10024431 |doi= 10.1006/mcpr.1998.0208
*cite journal | author=Santamaria R, Esposito G, Vitagliano L, "et al." |title=Functional and molecular modelling studies of two hereditary fructose intolerance-causing mutations at arginine 303 in human liver aldolase. |journal=Biochem. J. |volume=350 Pt 3 |issue= |pages= 823–8 |year= 2001 |pmid= 10970798 |doi=
*cite journal | author=Susan PP, Dunn WA |title=Starvation-induced lysosomal degradation of aldolase B requires glutamine 111 in a signal sequence for chaperone-mediated transport. |journal=J. Cell. Physiol. |volume=187 |issue= 1 |pages= 48–58 |year= 2001 |pmid= 11241348 |doi= 10.1002/1097-4652(2001)9999:9999<00::AID-JCP1050>3.0.CO;2-I |doilabel=10.1002/1097-4652(2001)9999:999900::AID-JCP10503.0.CO;2-I

External links

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