Pyridoxal 5'phosphate binding site of Escherichia coli beta cystathionase and cystathionine gamma synthase comparison of their sequences.
The phosphopyridoxyl peptides of beta cystathionase and cystathionine gamma synthase of Escherichia Coli were identified after reduction, carboxymethylation and proteolysis of the holoenzymes. Their comparison with those obtained from rat liver gamma cystathionase (Fearon, C.W., Rodkey, J.A. and Abeles R.H. 1982. Biochemistry 21 3790-3794.) showed a high degree of homology between the three PLP binding sites with the presence of the tripeptide sequence: Thr-Lys(Pxy)-Tyr in their structure. This homology suggests that these enzymes of methionine metabolism have probably the same origin.
Martel
A
A
Bouthier de la Tour
C
C
Le Goffic
F
F
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D019757:Carbon-Oxygen Lyases; D003542:Cystathionine gamma-Lyase / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D008099:Liver / Q000201:enzymology; D008190:Lyases / Q000378:metabolism*; D010446:Peptide Fragments; D011732:Pyridoxal Phosphate / Q000378:metabolism*; D051381:Rats; D013053:Spectrophotometry
D010446:Peptide Fragments; D011732:Pyridoxal Phosphate; C022696:O-succinylhomoserine (thiol)-lyase; D008190:Lyases; D019757:Carbon-Oxygen Lyases; D003542:Cystathionine gamma-Lyase