Disease relevance of Ald

• The results of E. coli expression of the mutated aldolase A enzyme confirmed the thermolabile nature of the abnormal enzyme [1].
• Human aldolase A deficiency associated with a hemolytic anemia: thermolabile aldolase due to a single base mutation [1].
• Fructose-1,6-bisphosphate aldolase A (fructose-bisphosphate aldolase; EC 4.1.2.13) deficiency is an autosomal recessive disorder associated with hereditary hemolytic anemia [1].

High impact information on Ald

• To further examine this possibility, the thermal stability of aldolase A of the patient and of a normal control, expressed in Escherichia coli using expression plasmids, was determined [1].
• Nucleotide analysis of the patient's aldolase A cDNA showed a substitution of a single nucleotide (adenine to guanine) at position 386 in a coding region [1].
• Two mRNAs encoding aldolase contain three exons and differ only in the poly(A) site [2].
• Alternate use of divergent forms of an ancient exon in the fructose-1,6-bisphosphate aldolase gene of Drosophila melanogaster [2].
• In addition, neither GAPDH nor aldolase colocalize at Z-discs and M-lines in the sarcomeres of muscles from GPDH-3 transgenic flies [3].

Biological context of Ald

• Alternative splicing of fructose 1,6-bisphosphate aldolase transcripts in Drosophila melanogaster predicts three isozymes [4].
• The complete amino acid sequence of FBP aldolase from Drosophila melanogaster has been determined [5].
• Genetic and cytogenetic studies of four glycolytic enzymes in Drosophila melanogaster: aldolase, triosephosphate isomerase, 3-phosphoglycerate kinase, and phosphoglucomutase [6].
• Active sites and substrate-binding determinant analysis suggest that the isolated enzyme in terms of function resembles type A aldolase [7].
• Nearly full-length cDNA clones for muscle-type and non-muscle-type aldolase mRNAs were cloned from lambda gt10 cDNA libraries constructed from skeletal muscle and liver mRNAs of lamprey (Entosphenus japonicus) [8].

Anatomical context of Ald

• In contrast with the ubiquitously expressed Ald gene, Bgm expression is restricted to the tissues that are affected by X-ALD such as brain, testis and adrenals [9].

Associations of Ald with chemical compounds

• The genes that encode fructose 1,6-bisphosphate aldolase of Drosophila melanogaster have been isolated and characterized [4].
• This stability may be related to the unusually low cysteine and histidine content of Drosophila aldolase [10].
• Biotin and fluorescent labeling of RNA using T4 RNA ligase [11].
• Biotin, fluorescein, and tetramethylrhodamine derivatives of P1-(6-aminohex-1-yl)-P2-(5'-adenosine) pyrophosphate were synthesized and used as substrates with T4 RNA ligase [11].
• Expression of fda in S. carnosus led to a six- to eightfold increase in aldolase production and activity; low levels of glucose in the growth medium stimulated activity [12].

Other interactions of Ald

• The nutritional conditions tested had little or no effect on the activities and transcript levels of ALD and PGK [13].

Analytical, diagnostic and therapeutic context of Ald

• Fructose 1,6-bisphosphate aldolase of Drosophila melanogaster: comparative sequence analyses around the substrate-binding lysyl residue [14].
• During mouse brain development, Bgm mRNA was first detected by Northern-blot analysis on embryonic day 18 and increased steadily towards adulthood, whereas the highest level of Ald mRNA was found on embryonic day 12 and decreased gradually during differentiation [9].
• Drosophila eIF-2 alpha has been identified by in vitro translation of T7 RNA polymerase-transcribed mRNA, and immunoblotting with anti-Drosophila eIF-2 alpha antiserum [15].
• Using immunocytochemistry, aldolase localized to the tegumental region of the adult worms [7].

References