Literature summary for 4.4.1.13 extracted from

Bertoldi, M.; Cellini, B.; Laurents, D.V.; Borri Voltattorni, C.
Folding pathway of the pyridoxal 5'-phosphate C-S lyase MalY from Escherichia coli (2005), Biochem. J., 389, 885-898.

General Stability

General Stability	Organism
the coenzyme strongly increases the protein stability. It is essential for the step involving dissociation of dimer into monomers and is not required for refolding of single monomers, but it is necessary to attain the native dimeric structure critical for the biological activities of MalY	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
urea-induced unfolding, unfolding proceeds in at least three stages.The first transition, occurring between 0 and 1 M urea, gives rise to a partially active dimeric species that binds pyridoxal 5'-phosphate. The second equilibrium transition involving dimer dissociation, release of pyridoxal 5'-phosphate and loss of lyase activity leads to the formation of a monomeric equilibrium intermediate. It is a partially unfolded molecule that retains most of the native-state secondary structure, binds significant amounts of 8-anilino-1-naphthalenesulfonic acid (a probe for exposed hydro-phobic surfaces) and tends to self-associate. The self-associated aggregates predominate at urea concentrations of 24 M for holoMalY. The third step represents the complete unfolding of the enzyme. Both holo-and apo-MalY can be successfully refolded into the active enzyme with an 85% yield. Large misfolded soluble aggregates cannot be refolded and can be responsible for the incomplete reactivation	Escherichia coli

Renatured (Comment)

Organism

urea-induced unfolding, unfolding proceeds in at least three stages.The first transition, occurring between 0 and 1 M urea, gives rise to a partially active dimeric species that binds pyridoxal 5'-phosphate. The second equilibrium transition involving dimer dissociation, release of pyridoxal 5'-phosphate and loss of lyase activity leads to the formation of a monomeric equilibrium intermediate. It is a partially unfolded molecule that retains most of the native-state secondary structure, binds significant amounts of 8-anilino-1-naphthalenesulfonic acid (a probe for exposed hydro-phobic surfaces) and tends to self-associate. The self-associated aggregates predominate at urea concentrations of 24 M for holoMalY. The third step represents the complete unfolding of the enzyme. Both holo-and apo-MalY can be successfully refolded into the active enzyme with an 85% yield. Large misfolded soluble aggregates cannot be refolded and can be responsible for the incomplete reactivation

Escherichia coli

Synonyms

Synonyms	Comment	Organism
MalY	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	the coenzyme strongly increases the protein stability. It is essential for the step involving dissociation of dimer into monomers and is not required for refolding of single monomers, but it is necessary to attain the native dimeric structure critical for the biological activities of MalY	Escherichia coli