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Structure paper

TitleStructural and kinetic studies on native intermediates and an intermediate analogue in benzoylformate decarboxylase reveal a least motion mechanism with an unprecedented short-lived predecarboxylation intermediate.
Journal, issue, pagesBiochemistry, Vol. 48, Page 3258-3268, Year 2009
Publish dateJan 26, 2009 (structure data deposition date)
AuthorsBruning, M. / Berheide, M. / Meyer, D. / Golbik, R. / Bartunik, H. / Liese, A. / Tittmann, K.
External linksBiochemistry / PubMed:19182954
MethodsX-ray diffraction
Resolution1.62 Å
Structure data

PDB-3fzn:
Intermediate analogue in benzoylformate decarboxylase
Method: X-RAY DIFFRACTION / Resolution: 1.62 Å

Chemicals

ChemComp-D7K:
3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-{(S)-hydroxy[(R)-hydroxy(methoxy)phosphoryl]phenylmethyl}-5-(2-{[(R)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium

ChemComp-MG:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-PO4:
PHOSPHATE ION

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-HOH:
WATER

Source
  • pseudomonas putida (bacteria)
KeywordsLYASE / benzoylformate decarboxylase / thiamin diphosphate / intermediate analogue / Aromatic hydrocarbons catabolism / Calcium / Decarboxylase / Magnesium / Mandelate pathway / Metal-binding / Thiamine pyrophosphate

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