• Publications
  • Influence
Allantoate amidinohydrolase (Allantoicase) from Chlamydomonas reinhardtii: its purification and catalytic and molecular characterization.
The effect of group-specific reagents suggest that the amino acids histidine, tyrosine, and cysteine are essentials for the allantoicase activity with both substrates.
Urea is a product of ureidoglycolate degradation in chickpea. Purification and characterization of the ureidoglycolate urea-lyase.
A ureidoglycolate-degrading activity was analyzed in different organs of chickpea, for the first time that such an activity is detected in plant tissues, and it is suggested that the enzyme is a metalloprotein.
Biochemical characterisation of an allantoate-degrading enzyme from French bean (Phaseolus vulgaris): the requirement of phenylhydrazine
The first time that an allantoate-degrading activity has been partially purified and characterised from a plant extract and the allosteric regulation of the enzyme suggests a critical role in the regulation of ureide degradation.
Degradation of ureidoglycolate in French bean (Phaseolus vulgaris) is catalysed by a ubiquitous ureidoglycolate urea-lyase
A ureidoglycolate-degrading activity was analysed in different tissues of French bean (Phaseolus vulgaris L.) plants during development, although values were very low in seeds before germination and in cotyledons, and the highest levels of specific activity were found in developing fruits.
An alternative pathway for ureide usage in legumes: enzymatic formation of a ureidoglycolate adduct in Cicer arietinum and Phaseolus vulgaris.
It was demonstrated that purified ureidoglycolases from chickpea and French bean do not produce glyoxylate, and can use phenylhydrazine as a substrate with K(m) values of 4.0 mM and 8.5 mM, which supports their former classification as ureIDoglycolate urea-lyases.