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PDBsum entry 6tcc
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Unknown function
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PDB id
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6tcc
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References listed in PDB file
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Key reference
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Title
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Two novel fish paralogs provide insights into the rid family of imine deaminases active in pre-Empting enamine/imine metabolic damage.
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Authors
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S.Digiovanni,
C.Visentin,
G.Degani,
A.Barbiroli,
M.Chiara,
L.Regazzoni,
F.Di pisa,
A.J.Borchert,
D.M.Downs,
S.Ricagno,
M.A.Vanoni,
L.Popolo.
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Ref.
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Sci Rep, 2020,
10,
10135.
[DOI no: ]
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PubMed id
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Abstract
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Reactive Intermediate Deaminase (Rid) protein superfamily includes eight
families among which the RidA is conserved in all domains of life. RidA proteins
accelerate the deamination of the reactive 2-aminoacrylate (2AA), an enamine
produced by some pyridoxal phosphate (PLP)-dependent enzymes. 2AA accumulation
inhibits target enzymes with a detrimental impact on fitness. As a consequence
of whole genome duplication, teleost fish have two ridA paralogs, while other
extant vertebrates contain a single-copy gene. We investigated the biochemical
properties of the products of two paralogs, identified in Salmo salar.
SsRidA-1 and SsRidA-2 complemented the growth defect of a
Salmonella enterica ridA mutant, an in vivo model of 2AA stress. In vitro, both
proteins hydrolyzed 2-imino acids (IA) to keto-acids and ammonia.
SsRidA-1 was active on IA derived from nonpolar amino acids and
poorly active or inactive on IA derived from other amino acids tested. In
contrast, SsRidA-2 had a generally low catalytic efficiency, but
showed a relatively higher activity with IA derived from L-Glu and aromatic
amino acids. The crystal structures of SsRidA-1 and
SsRidA-2 provided hints of the remarkably different conformational
stability and substrate specificity. Overall, SsRidA-1 is similar to
the mammalian orthologs whereas SsRidA-2 displays unique properties
likely generated by functional specialization of a duplicated ancestral gene.
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