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Chemical Compound Review: 

PubChem22630     pyridin-2-ylhydrazine

Synonyms: SureCN122616, ACMC-1AKBY, Enamine_005250, H17082_ALDRICH, AG-F-65464, ...
 
 
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Disease relevance of pyridin-2-ylhydrazine

  • The crystal structure of the complex between the copper amine oxidase from Escherichia coli (ECAO) and a covalently bound inhibitor, 2-hydrazinopyridine, has been determined to a resolution of 2.0 A [1].
 

High impact information on pyridin-2-ylhydrazine

  • Active site rearrangement of the 2-hydrazinopyridine adduct in Escherichia coli amine oxidase to an azo copper(II) chelate form: a key role for tyrosine 369 in controlling the mobility of the TPQ-2HP adduct [2].
  • The steady state kinetics of aminomethyl- and aminoethylpyridines confirm that the formation of the product Schiff base, analogous to the azo form of the 2-hydrazinopyridine adduct, is not hindered in solution [3].
  • The structure of an adduct of SSAO and the irreversible inhibitor 2-hydrazinopyridine has been solved and refined to 2.9 A resolution [4].
 

Biological context of pyridin-2-ylhydrazine

  • Reaction of the enzyme with the irreversible inhibitor 2-hydrazinopyridine (2-HP) reveals differences in the reactivity of Y369F compared with wild type with more efficient formation of an adduct (lambda(max) = 525 nm) perhaps reflecting increased mobility of the TPQ adduct within the active site of Y369F [5].

References

  1. Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction. Wilmot, C.M., Murray, J.M., Alton, G., Parsons, M.R., Convery, M.A., Blakeley, V., Corner, A.S., Palcic, M.M., Knowles, P.F., McPherson, M.J., Phillips, S.E. Biochemistry (1997) [Pubmed]
  2. Active site rearrangement of the 2-hydrazinopyridine adduct in Escherichia coli amine oxidase to an azo copper(II) chelate form: a key role for tyrosine 369 in controlling the mobility of the TPQ-2HP adduct. Mure, M., Kurtis, C.R., Brown, D.E., Rogers, M.S., Tambyrajah, W.S., Saysell, C., Wilmot, C.M., Phillips, S.E., Knowles, P.F., Dooley, D.M., McPherson, M.J. Biochemistry (2005) [Pubmed]
  3. The metal function in the reactions of bovine serum amine oxidase with substrates and hydrazine inhibitors. De Matteis, G., Agostinelli, E., Mondovì, B., Morpurgo, L. J. Biol. Inorg. Chem. (1999) [Pubmed]
  4. Structure of human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1. Jakobsson, E., Nilsson, J., Ogg, D., Kleywegt, G.J. Acta Crystallogr. D Biol. Crystallogr. (2005) [Pubmed]
  5. Conserved tyrosine-369 in the active site of Escherichia coli copper amine oxidase is not essential. Murray, J.M., Kurtis, C.R., Tambyrajah, W., Saysell, C.G., Wilmot, C.M., Parsons, M.R., Phillips, S.E., Knowles, P.F., McPherson, M.J. Biochemistry (2001) [Pubmed]
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