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Aldolase B is a homotetrameric enzyme, composed of four subunits with molecular weights of 36 kDa with local 222 symmetry. Each subunit has a molecular weight of 36 kDa and contains an eight-stranded α/β barrel, which encloses lysine 229 (the Schiff-base forming amino acid that is key for catalysis).
Some defects in aldolase B cause hereditary fructose intolerance. The metabolism of free fructose in liver exploits the ability of aldolase B to use fructose 1-phosphate as a substrate. [6] Archaeal fructose-bisphosphate aldolase/phosphatase is presumably involved in gluconeogenesis because its product is fructose 6-phosphate. [7]
Aldolase A (ALDOA, or ALDA), also known as fructose-bisphosphate aldolase, is an enzyme that in humans is encoded by the ALDOA gene on chromosome 16.. The protein encoded by this gene is a glycolytic enzyme that catalyzes the reversible conversion of fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP).
Unqualified, aldolase usually refers to the enzyme fructose-bisphosphate aldolase. Aldolase may also refer to: Proteins serving as fructose-bisphosphate aldolase
11676 Ensembl ENSG00000109107 ENSMUSG00000017390 UniProt P09972 P05063 RefSeq (mRNA) NM_005165 NM_009657 NM_001303423 RefSeq (protein) NP_005156 NP_001290352 NP_033787 Location (UCSC) Chr 17: 28.57 – 28.58 Mb Chr 11: 78.21 – 78.22 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Aldolase C, fructose-bisphosphate (ALDOC, or ALDC), is an enzyme that, in humans, is encoded by the ...
Because fructokinase has a high Vmax fructose entering cells is quickly phosphorylated to fructose 1-phosphate. [1] In this form it is usually accumulated in the liver until it undergoes further conversion by aldolase B (the rate limiting enzyme of fructose metabolism). Aldolase B converts it into glyceraldehyde and dihydroxyacetone phosphate ...
Common names include decarboxylase, dehydratase, aldolase, etc. When the product is more important, synthase may be used in the name, e.g. phosphosulfolactate synthase (EC 4.4.1.19, Michael addition of sulfite to phosphoenolpyruvate). A combination of both an elimination and a Michael addition is seen in O-succinylhomoserine (thiol)-lyase (MetY ...
It is proposed that fructose 1,6-bisphosphate aldolase/phosphatase was an ancestral gluconeogenic enzyme and had preceded glycolysis. [37] However, a prebiotic glycolysis would follow the same chemical mechanisms as gluconeogenesis, due to microscopic reversibility, and in this view would have occurred at the same time.