By P.M. Jordan (Eds.)
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Extra resources for Biosynthesis of Tetrapyrroles
This mechanism explains why no amino donor other than the substrate is required. The likely involvement of the cyclic glutamate semialdehyde intermediate (HAT) as a substrate need not affect the above mechanism since the transaminase would catalyse ring opening as the first step in the mechanism. Such ring opening (mutarotation) occurs routinely in enzymic transformations involving glucose and other sugars. Most recently the aminotransferase cDNA has been isolated from barley [ 1261and the derived protein sequence has been shown to be similar to that of Salmonella typhimurium .
In the absence of uroporphyrinogen I11 synthase, the highly reactive preuroporphyrinogen cyclises without rearrangement, in a non enzymic reaction, to give uroporphyrinogen I. Since many of the studies on the deaminase and synthase (cosynthase) have been closely interwoven, the two enzymes will be considered in this section together. Their combined reactions are shown below in Scheme 9. The enzymic production of uroporphyrinogen I11 from porphobilinogen was first demonstrated by Bogorad and Granick [ 1841 using enzyme extracts from spinach.
It is suggested that the zinc, ligands comprise twohhree histidine nitrogens, two oxygen ligands (tyrosine, aspartate or water) and one cysteine sulphur. The zinc, coordination comprises four sulphur ligands. The interesting possibility that the putative metal-binding amino acid sequence can interact with the zinc in two ways has been proposed to explain the EXAFS data. The differences in the folding of the metal-binding sequence are attributed to induced asymetry in the interaction between monomers in the dimers .
Biosynthesis of Tetrapyrroles by P.M. Jordan (Eds.)