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Structure paper

TitleIsotope effects reveal that para-substituted benzylamines are poor reactivity probes of the quinoprotein mechanism for aromatic amine dehydrogenase.
Journal, issue, pagesBiochemistry, Vol. 46, Page 9250-9259, Year 2007
Publish dateJun 30, 2006 (structure data deposition date)
AuthorsHothi, P. / Roujeinikova, A. / Khadra, K.A. / Lee, M. / Cullis, P. / Leys, D. / Scrutton, N.S.
External linksBiochemistry / PubMed:17636875
MethodsX-ray diffraction
Resolution1.6 - 1.85 Å
Structure data

PDB-2hj4:
Crystal structure of Alcaligenes faecalis AADH complex with p-nitrobenzylamine
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-2hjb:
Crystal structure of Alcaligenes faecalis AADH in complex with p-methoxybenzylamine
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-2q7q:
Crystal structure of Alcaligenes faecalis AADH in complex with p-chlorobenzylamine.
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

Chemicals

ChemComp-PNZ:
P-NITRO-BENZYLAMINE

ChemComp-HOH:
WATER

ChemComp-PZM:
1-(4-METHOXYPHENYL)METHANAMINE

ChemComp-C2B:
1-(4-CHLOROPHENYL)METHANAMINE

Source
  • alcaligenes faecalis (bacteria)
KeywordsOXIDOREDUCTASE / kinetic isotope effect / p-substituted benzylamines / p-substituted benzylamines; oxidoreductase / TTQ

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