Characterization of prolidase I and II purified from normal human erythrocytes: comparison with prolidase in erythrocytes from a patient with prolidase deficiency.
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| Abstract |
The effect of various sulfur-containing amino acids on the activities of prolidase isoenzymes I and II isolated from erythrocytes of healthy individuals, and erythrocyte lysates from a patient with prolidase deficiency was investigated. The activity of prolidase I against glycylproline was strongly enhanced by D: -methionine. L: -Methionine and D: ,L: -methionine slightly enhanced the activity at low concentration, but N-acetyl-L: -methionine had no effect. D: -Ethionine, L: -ethionine, and D: ,L: -ethionine also enhanced the activity of prolidase I. D: ,L: -Homocysteine enhanced the activity at low concentration, but inhibited the activity at 50 mM: . The activity of prolidase II against methionylproline was enhanced by D: -methionine, D: ,L: -methionine, and L: -methionine, but N-acetyl-L: -methionine had no effect. D: -Ethionine and D: ,L: -ethionine strongly enhanced the activity of prolidase II compared with L: -ethionine; D: ,L: -homocysteine weakly enhanced the activity. D: ,L: -Homocysteine-thiolactone inhibited the activities of prolidase I and II in a concentration-dependent manner. The effect of various sulfur-containing amino acids on prolidase activity against methionylproline in erythrocyte lysates from a patient with prolidase deficiency was almost the same as that on prolidase II. The kinetics of the activities of prolidase I, II, and patient prolidase were also studied. Their K (m) values were changed by adding sulfur-containing amino acids, but V (max) values were unchanged.
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| Authors | Soichiro Uramatsu, Gang Liu, Qing Yang, Mutsumi Uramatsu, Haidong Chi, Jincai Lu, Koichi Yamashita, Hiroyuki Kodama |
| Journal | Amino acids (Amino Acids) Vol. 37 Issue 3 Pg. 543-51 (Sep 2009) ISSN: 1438-2199 [Electronic] Austria |
| PMID | 19263194 (Publication Type: Journal Article) |
| Chemical References |
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