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Structure and mechanism of HpcH: a metal ion dependent class II aldolase from the homoprotocatechuate degradation pathway of Escherichia coli.

Rea D, Fülöp V, Bugg TD, Roper DI
J Mol Biol 373 866-76 (2007)
Cited: 11 times
EuropePMC logo PMID: 17881002

Abstract

Microorganisms are adept at degrading chemically resistant aromatic compounds. One of the longest and most well characterized aromatic catabolic pathways is the 4-hydroxyphenylacetic acid degradation pathway of Escherichia coli. The final step involves the conversion of 4-hydroxy-2-oxo-heptane-1,7-dioate into pyruvate and succinic semialdehyde. This reaction is catalyzed by 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (HpcH), a member of the divalent metal ion dependent class II aldolase enzymes that have great biosynthetic potential. We have solved the crystal structure of HpcH in the apo form, and with magnesium and the substrate analogue oxamate bound, to 1.6 A and 2.0 A, respectively. Comparison with similar structures of the homologous 2-dehydro-3-deoxygalactarate aldolase, coupled with site-directed mutagenesis data, implicate histidine 45 and arginine 70 as key catalytic residues.

Articles - 2v5k mentioned but not cited (2)

  1. Structural and kinetic characterization of 4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate aldolase, a protocatechuate degradation enzyme evolutionarily convergent with the HpaI and DmpG pyruvate aldolases. Wang W, Mazurkewich S, Kimber MS, Seah SY. J Biol Chem 285 36608-36615 (2010)
  2. On the use of logarithmic scales for analysis of diffraction data. Urzhumtsev A, Afonine PV, Adams PD. Acta Crystallogr D Biol Crystallogr 65 1283-1291 (2009)


Articles citing this publication (9)

  1. Evolution of enzymatic activities in the enolase superfamily: L-rhamnonate dehydratase. Rakus JF, Fedorov AA, Fedorov EV, Glasner ME, Hubbard BK, Delli JD, Babbitt PC, Almo SC, Gerlt JA. Biochemistry 47 9944-9954 (2008)
  2. Chemoenzymatic Platform for Synthesis of Chiral Organofluorines Based on Type II Aldolases. Fang J, Hait D, Head-Gordon M, Chang MCY. Angew Chem Int Ed Engl 58 11841-11845 (2019)
  3. Recent trends in the stereoselective synthesis of (poly)-substituted 2-oxo acids by biocatalyzed aldol reaction. Pickl M. Curr Opin Green Sustain Chem 30 100476 (2021)
  4. Crystal structure of reaction intermediates in pyruvate class II aldolase: substrate cleavage, enolate stabilization, and substrate specificity. Coincon M, Wang W, Sygusch J, Seah SY. J Biol Chem 287 36208-36221 (2012)
  5. Structural and Kinetic Characterization of the 4-Carboxy-2-hydroxymuconate Hydratase from the Gallate and Protocatechuate 4,5-Cleavage Pathways of Pseudomonas putida KT2440. Mazurkewich S, Brott AS, Kimber MS, Seah SY. J Biol Chem 291 7669-7686 (2016)
  6. SbnG, a citrate synthase in Staphylococcus aureus: a new fold on an old enzyme. Kobylarz MJ, Grigg JC, Sheldon JR, Heinrichs DE, Murphy ME. J Biol Chem 289 33797-33807 (2014)
  7. The role of a conserved histidine residue in a pyruvate-specific Class II aldolase. Wang W, Seah SY. FEBS Lett 582 3385-3388 (2008)
  8. Catalytic and structural insights into a stereospecific and thermostable Class II aldolase HpaI from Acinetobacter baumannii. Watthaisong P, Binlaeh A, Jaruwat A, Lawan N, Tantipisit J, Jaroensuk J, Chuaboon L, Phonbuppha J, Tinikul R, Chaiyen P, Chitnumsub P, Maenpuen S. J Biol Chem 297 101280 (2021)
  9. Investigation into the Mode of Phosphate Activation in the 4-Hydroxy-4-Methyl-2-Oxoglutarate/4-Carboxy-4-Hydroxy-2-Oxoadipate Aldolase from Pseudomonas putida F1. Mazurkewich S, Seah SY. PLoS One 11 e0164556 (2016)


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