Pub. Date : 2004 Nov 26
PMID : 15364907
8 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
1 | The KAT-I isozyme has also been reported to possess beta-lyase activity toward several sulfur- and selenium-conjugated molecules, leading to the proposal of a role of the enzyme in carcinogenesis associated with environmental pollutants. | Sulfur | kynurenine aminotransferase 1 | Homo sapiens |
2 | The KAT-I isozyme has also been reported to possess beta-lyase activity toward several sulfur- and selenium-conjugated molecules, leading to the proposal of a role of the enzyme in carcinogenesis associated with environmental pollutants. | Selenium | kynurenine aminotransferase 1 | Homo sapiens |
3 | We solved the structure of human KAT-I in its 5"-pyridoxal phosphate and pyridoxamine phosphate forms and in complex with the competing substrate l-Phe. | 5"-pyridoxal phosphate | kynurenine aminotransferase 1 | Homo sapiens |
4 | We solved the structure of human KAT-I in its 5"-pyridoxal phosphate and pyridoxamine phosphate forms and in complex with the competing substrate l-Phe. | pyridoxamine phosphate | kynurenine aminotransferase 1 | Homo sapiens |
5 | We solved the structure of human KAT-I in its 5"-pyridoxal phosphate and pyridoxamine phosphate forms and in complex with the competing substrate l-Phe. | Phenylalanine | kynurenine aminotransferase 1 | Homo sapiens |
6 | Our data reveal a key structural role of Glu(27), providing a molecular basis for the reported loss of enzymatic activity displayed by the equivalent Glu --> Gly mutation in KAT-I of spontaneously hypertensive rats. | Glutamic Acid | kynurenine aminotransferase 1 | Homo sapiens |
7 | Our data reveal a key structural role of Glu(27), providing a molecular basis for the reported loss of enzymatic activity displayed by the equivalent Glu --> Gly mutation in KAT-I of spontaneously hypertensive rats. | Glutamic Acid | kynurenine aminotransferase 1 | Homo sapiens |
8 | Our data reveal a key structural role of Glu(27), providing a molecular basis for the reported loss of enzymatic activity displayed by the equivalent Glu --> Gly mutation in KAT-I of spontaneously hypertensive rats. | Glycine | kynurenine aminotransferase 1 | Homo sapiens |