Title : Crystal structure of human kynurenine aminotransferase I.

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