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- W104002020 abstract "Introduction L-amino acid oxidase (LAAO) occurs in many different organisms such as bacteria (Corynebacterium, Proteus rettgeri), cyanobacteria (Synechococcus), fungi (Neurospora crassa), green algae (Chlamydomonas rheinhardtii) and most prominently, venomonous snakes (such as Crotalidae and Viperidae). Ophidian LAAOs contribute to the toxicity of snake venom while in all other cases the enzyme appears to be involved in utilisation of ammonia as a nitrogen source. There are also major differences in molecular weight, substrate specificity, glycosylation and the physiological regulation of LAAO. In view of this diversity it can be envisaged that these proteins evolved from different ancestral proteins. In order to aid investigations aimed at the elucidation ofthe three-dimensional structure and the analysis ofthe oligosaccharide moiety of LAAO from the Malayan pit viper (Calloselasma rhodostoma) we have cloned and sequenced the gene from a cDNA library. Here we report the phylogenetic relationship of C. rhodostoma LAAO to other FAD-dependent oxidases and describe a highly conserved FAD binding fold." @default.
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- W104002020 date "1999-01-01" @default.
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- W104002020 title "Comparison of the amino acid sequence or Calloselasma rhodostoma L-amino acid oxidase to other FAD-dependent oxidases" @default.
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