Crystallization (Comment) | Organism |
---|---|
native and modified enzyme, X-ray diffraction structure determination and analysis at 1.7 A resolution | Schizosaccharomyces pombe |
Protein Variants | Comment | Organism |
---|---|---|
additional information | the yeast enzyme is covalently modified with dehydroalanine derived from its natural substrate serine, giving a serine racemase with catalytically active lysinoalanyl residue. The modification is not reversed by incubation in 20 mM potassium phosphate buffer, pH 7.2, without serine for several days at room temperature. The enzyme remains partially active even though its essential Lys57 inherently forming a Schiff base with the coenzyme pyridoxal 5'-phosphate is converted to N(6)-(R-2-amino-2-carboxyethyl)-L-lysyl (lysino-D-alanyl) residue. The alpha-amino group of the D-alanyl moiety of the lysino-D-alanyl residue serves as a catalytic base in the same manner asthe epsilon-amino group of Lys57 of the original enzyme. The specific activities of modified spSR for L-serine racemization and L-serine dehydration are 54%, and 68%, respectively, of those of the original spSR | Schizosaccharomyces pombe |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-serine | Schizosaccharomyces pombe | - |
D-serine | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Schizosaccharomyces pombe | O59791 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
L-serine = D-serine | reaction mechanism, overview | Schizosaccharomyces pombe |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-serine | - |
Schizosaccharomyces pombe | D-serine | - |
? |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | - |
Schizosaccharomyces pombe |