Protein Family Models

Transaldolase (TAL) is an enzyme of the pentose phosphate pathway (PPP) found almost ubiquitously in the three domains of life (Archaea, Bacteria, and Eukarya). TAL shares a high degree of structural similarity and sequence identity with fructose-6-phosphate aldolase (FSA). They both belong to the class I aldolase family[4]. Their protein structures have been revealed[5]. [1]. 11705376. Snapshots of catalysis: the structure of fructose-1,6-(bis)phosphate aldolase covalently bound to the substrate dihydroxyacetone phosphate. Choi KH, Shi J, Hopkins CE, Tolan DR, Allen KN;. Biochemistry 2001;40:13868-13875. [2]. 11298760. Identification of catalytically important residues in the active site of Escherichia coli transaldolase. Schorken U, Thorell S, Schurmann M, Jia J, Sprenger GA, Schneider G;. Eur J Biochem 2001;268:2408-2415. [3]. 10869557. The three-dimensional structure of human transaldolase. Thorell S, Gergely P Jr, Banki K, Perl A, Schneider G. FEBS Lett 2000;475:205-208. [4]. 26131847. Converting Transaldolase into Aldolase through Swapping of the Multifunctional Acid-Base Catalyst: Common and Divergent Catalytic Principles in F6P Aldolase and Transaldolase. Sautner V, Friedrich MM, Lehwess-Litzmann A, Tittmann K;. Biochemistry. 2015;54:4475-4486. [5]. 25267444. Sweet siblings with different faces: the mechanisms of FBP and F6P aldolase, transaldolase, transketolase and phosphoketolase revisited in light of recent structural data. Tittmann K;. Bioorg Chem. 2014;57:263-280. (from Pfam)

Date:

2024-10-16

fructose-6-phosphate aldolase catalyzes the reversible formation of fructose 6-phosphate from dihydroxyacetone and D-glyceraldehyde 3-phosphate via an aldolization reaction

Date:

2020-11-18

Date:

2021-10-28