Vitamin B(6)-dependent enzymes may be grouped into five evolutionarily unrelated families, each having a different fold. Within fold type I enzymes, L-threonine aldolase (L-TA) and fungal alanine racemase (AlaRac) belong to a subgroup of structurally and mechanistically closely related proteins, which specialised during evolution to perform different functions. In a previous study, a comparison of the catalytic properties and active site structures of these enzymes suggested that they have a catalytic apparatus with the same basic features. Recently, recombinant D-threonine aldolases (D-TAs) from two bacterial organisms have been characterised, their predicted amino acid sequences showing no significant similarities to any of the known B(6) enzymes. In the present work, a comparative structural analysis suggests that D-TA has an alpha/beta barrel fold and therefore is a fold type III B(6) enzyme, as eukaryotic ornithine decarboxylase (ODC) and bacterial AlaRac. The presence of both TA and AlaRac in two distinct evolutionary unrelated families represents a novel and interesting example of convergent evolution. The independent emergence of the same catalytic properties in families characterised by completely different folds may have not been determined by chance, but by the similar structural features required to catalyse pyridoxal phosphate-dependent aldolase and racemase reactions.

Threonine aldolase and alanine racemase: novel examples of convergent evolution in the superfamily of vitamin B6-dependent enzymes / Paiardini, Alessandro; Contestabile, Roberto; D'Aguanno, Simona; Pascarella, Stefano; Bossa, Francesco. - In: BIOCHIMICA ET BIOPHYSICA ACTA. - ISSN 0006-3002. - STAMPA. - 1647:(2003), pp. 214-219. [10.1016/S1570-9639(03)00050-5]

Threonine aldolase and alanine racemase: novel examples of convergent evolution in the superfamily of vitamin B6-dependent enzymes

PAIARDINI, ALESSANDRO;CONTESTABILE, Roberto;D'AGUANNO, SIMONA;PASCARELLA, Stefano;BOSSA, Francesco
2003

Abstract

Vitamin B(6)-dependent enzymes may be grouped into five evolutionarily unrelated families, each having a different fold. Within fold type I enzymes, L-threonine aldolase (L-TA) and fungal alanine racemase (AlaRac) belong to a subgroup of structurally and mechanistically closely related proteins, which specialised during evolution to perform different functions. In a previous study, a comparison of the catalytic properties and active site structures of these enzymes suggested that they have a catalytic apparatus with the same basic features. Recently, recombinant D-threonine aldolases (D-TAs) from two bacterial organisms have been characterised, their predicted amino acid sequences showing no significant similarities to any of the known B(6) enzymes. In the present work, a comparative structural analysis suggests that D-TA has an alpha/beta barrel fold and therefore is a fold type III B(6) enzyme, as eukaryotic ornithine decarboxylase (ODC) and bacterial AlaRac. The presence of both TA and AlaRac in two distinct evolutionary unrelated families represents a novel and interesting example of convergent evolution. The independent emergence of the same catalytic properties in families characterised by completely different folds may have not been determined by chance, but by the similar structural features required to catalyse pyridoxal phosphate-dependent aldolase and racemase reactions.
2003
Vitamin B(6)-dependent enzymes; L-threonine aldolase; alanine racemase
01 Pubblicazione su rivista::01a Articolo in rivista
Threonine aldolase and alanine racemase: novel examples of convergent evolution in the superfamily of vitamin B6-dependent enzymes / Paiardini, Alessandro; Contestabile, Roberto; D'Aguanno, Simona; Pascarella, Stefano; Bossa, Francesco. - In: BIOCHIMICA ET BIOPHYSICA ACTA. - ISSN 0006-3002. - STAMPA. - 1647:(2003), pp. 214-219. [10.1016/S1570-9639(03)00050-5]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/251097
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