Skip to main content
padlock icon - secure page this page is secure

Crystallization and preliminary X‐ray crystallographic analysis of 2‐methyl‐3‐hydroxypyridine‐5‐carboxylic acid (MHPC) oxygenase from Pseudomonas sp. MA‐1

Buy Article:

$52.00 + tax (Refund Policy)

2‐Methyl‐3‐hydroxypyridine‐5‐carboxylic acid (MHPC) oxygenase (MHPCO) catalyzes the conversion of an aromatic substrate, MHPC, to an aliphatic compound, α‐(N‐acetylaminomethylene)‐succinic acid, and is involved in the degradation of vitamin B6 by the soil bacterium Pseudomonas sp. MA‐1. Using only FAD as a cofactor, MHPCO is unique in catalyzing hydroxylation and subsequent aromatic ring cleavage without requiring a metal‐ion cofactor. Here, the crystallization of MHPCO is reported together with preliminary X‐ray crystallographic data. An MHPCO crystal obtained by hanging‐drop vapour diffusion diffracted X‐rays to 2.25 Å resolution and belonged to the triclinic space group P1, with four molecules per asymmetric unit.
No References
No Citations
No Supplementary Data
No Article Media
No Metrics

Keywords: MHPCO; Pseudomonas sp. MA‐1; aromatic flavoprotein monooxygenase; aromatic ring cleavage; hydroxypyridine

Document Type: Research Article

Publication date: March 1, 2005

  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more