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Arabinose 5-phosphate covalently inhibits transaldolase.

Light SH, Anderson WF
J Struct Funct Genomics 15 41-4 (2014)
Cited: 7 times
EuropePMC logo PMID: 24510200

Abstract

Arabinose 5-phosphate (A5P) is the aldopentose version of the ketohexose fructose 6-phosphate (F6P), having identical stereochemistry but lacking atoms corresponding to the 1-carbon and 1-hydroxyl. Despite structural similarity and conservation of the reactive portion of F6P, F6P acts as a substrate whereas A5P is reported to be an inhibitor of transaldolase. To address the lack of A5P reactivity we determined a crystal structure of the Francisella tularensis transaldolase in complex with A5P. This structure reveals that like F6P, A5P forms a covalent Schiff base with active site Lys135. Unlike F6P, A5P binding fails to displace an ordered active site water molecule. Retaining this water necessitates conformational changes at the A5P-protein linkage that possibly hinder reactivity. The findings presented here show the basis of A5P inhibition and suggest an unusual mechanism of competitive, reversible-covalent transaldolase regulation.

Reviews - 3upb mentioned but not cited (1)

  1. Recent advances in design of new urease inhibitors: A review. Kafarski P, Talma M. J Adv Res 13 101-112 (2018)


Reviews citing this publication (2)

  1. The Pentose Phosphate Pathway Dynamics in Cancer and Its Dependency on Intracellular pH. Alfarouk KO, Ahmed SBM, Elliott RL, Benoit A, Alqahtani SS, Ibrahim ME, Bashir AHH, Alhoufie STS, Elhassan GO, Wales CC, Schwartz LH, Ali HS, Ahmed A, Forde PF, Devesa J, Cardone RA, Fais S, Harguindey S, Reshkin SJ. Metabolites 10 E285 (2020)
  2. 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 57 263-280 (2014)

Articles citing this publication (4)

  1. Wide range of metabolic adaptations to the acquisition of the Calvin cycle revealed by comparison of microbial genomes. Asplund-Samuelsson J, Hudson EP. PLoS Comput Biol 17 e1008742 (2021)
  2. Identification of a d-Arabinose-5-Phosphate Isomerase in the Gram-Positive Clostridium tetani. Cech DL, Markin K, Woodard RW. J Bacteriol 199 e00246-17 (2017)
  3. Inhibition by fructose 1,6-bisphosphate of transaldolase from Escherichia coli. Ogawa T, Murakami K, Yoshino M. FEMS Microbiol Lett 363 fnw183 (2016)
  4. Novel mode of inhibition by D-tagatose 6-phosphate through a Heyns rearrangement in the active site of transaldolase B variants. Stellmacher L, Sandalova T, Schneider S, Schneider G, Sprenger GA, Samland AK. Acta Crystallogr D Struct Biol 72 467-476 (2016)


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