cystathionine L-homocysteine-lyase (deaminating)
L-cystathionine L-homocysteine-lyase (deaminating)
Cloning, purification, and crystallization of Escherichia coli cystathionine beta-lyase.
Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 A.
Slow-binding inhibition of Escherichia coli cystathionine beta-lyase by L-aminoethoxyvinylglycine: a kinetic and X-ray study.
Mode of action of cystathionine beta-lyase.
The crystal structure of cystathionine gamma-synthase from Nicotiana tabacum reveals its substrate and reaction specificity.
Crystal structure of a NifS-like protein from Thermotoga maritima: implications for iron sulphur cluster assembly.
The three-dimensional structure of cystathionine beta-lyase from Arabidopsis and its substrate specificity.
Although the residues 85-131 of 1ibj (PDB) are included in the first domain, the region seems to correspond to the first domain of 1cl1 and 1cl2. According to the literature [2], [4] & [7], this enzyme catalyzes the following reactions: (A) Formation of external aldimine (transaldimine), (B) Elimination of homocysteine, (C) Formation of internal aldimine (transaldimine), (D) Hydration of iminopropionate, to form pyruvate and ammonia, outside the enzyme. (This hydration might involve Schiff-base deforming reaction.)