Purification and properties of porphobilinogen deaminase from Arabidopsis thaliana. | Zendy

Russell M. Jones | Zendy; Peter M. Jordan | Zendy

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Purification and properties of porphobilinogen deaminase from Arabidopsis thaliana.

Author(s) -

Russell M. Jones,

Peter M. Jordan

Publication year - 1994

Publication title -

biochemical journal

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.706

H-Index - 265

eISSN - 1470-8728

pISSN - 0264-6021

DOI - 10.1042/bj2990895

Subject(s) - porphobilinogen deaminase , hydroxylamine , biochemistry , chemistry , porphobilinogen , enzyme , histidine , chromatography , reagent , arginine , stereochemistry , amino acid , organic chemistry , heme

Porphobilinogen deaminase (EC 4.3.1.8) has been purified to homogeneity (16,000-fold) from the plant Arabidopsis thaliana in yields of 8%. The deaminase is a monomer of M(r) 35,000, as shown by SDS/PAGE, and 31,000, using gel-filtration chromatography. The pure enzyme has a Vmax. of 4.5 mumol/h per mg and a Km of 17 +/- 4 microM. Determination of the pI and pH optimum revealed values of 5.2 and 8.0 respectively. The sequence of the N-terminus was found to be NH2-XVAVEQKTRTAI. The deaminase is heat-stable up to 70 degrees C and is inhibited by NH3 and hydroxylamine. The enzyme is inactivated by arginine-, histidine- and lysine-specific reagents. Incubation with the substrate analogue and suicide inhibitor, 2-bromoporphobilinogen, results in chain termination and in inactivation.

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