Literature summary for 4.3.1.18 extracted from

Baldassarre, M.; Scire, A.; Fiume, I.; Tanfani, F.
Insights into the structural properties of D-serine dehydratase from Saccharomyces cerevisiae: an FT-IR spectroscopic and in silico approach (2011), Biochimie, 93, 542-548.

Crystallization (Commentary)

Crystallization (Comment)	Organism
homology model of Dsd. In this model, Dsd adopts a fold that is characteristic of type III pyridoxal-dependent enzymes, consisting of an alpha/beta TIM-barrel and a beta-sandwich domain at the N- and C-termini, respectively. Analysis of the Amide I and Amide III infrared bands reveals that the amounts of 24% alpha, 29% b and 47% unordered structures correlate well with those derived from the model, 25%, 29% and 46% respectively	Saccharomyces cerevisiae

Crystallization (Comment)

Organism

homology model of Dsd. In this model, Dsd adopts a fold that is characteristic of type III pyridoxal-dependent enzymes, consisting of an alpha/beta TIM-barrel and a beta-sandwich domain at the N- and C-termini, respectively. Analysis of the Amide I and Amide III infrared bands reveals that the amounts of 24% alpha, 29% b and 47% unordered structures correlate well with those derived from the model, 25%, 29% and 46% respectively

Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	Dsd adopts a fold that is characteristic of type III pyridoxal-dependent enzymes	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)