HD-PTP is a catalytically inactive tyrosine phosphatase due to a conserved divergence in its phosphatase domain.
|Abstract||The HD-PTP protein has been described as a tumor suppressor candidate and based on its amino acid sequence, categorized as a classical non-transmembrane protein tyrosine phosphatase (PTP). To date, no HD-PTP phosphorylated substrate has been identified and controversial results concerning its catalytic activity have been recently reported.|
|Author||Gingras, Marie-Claude; Zhang, Yu Ling; Kharitidi, Dmitri; et al|
|Subject||Amino Acid Sequence Catalysis Cell Line Conserved Sequence DNA, Complementary Humans Kinetics Protein Tyrosine Phosphatases, Non-Receptor Sequence Homology, Amino Acid chemistry genetics metabolism|
Analysis of the substrate-binding site of human carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis.
|Abstract||Human carbonyl reductase is a member of the short-chain dehydrogenase/reductase (SDR) protein superfamily and is known to play an important role in the detoxification of xenobiotics bearing a carbonyl group. The two monomeric NADPH-dependent human isoforms of cytosolic carbonyl reductase CBR1 and CBR3 show a sequence similarity of 85% on the amino acid level, which is definitely high if compared to the low similarities usually observed among othe ... [truncated at 450 characters in length]|
|Author||El-Hawari, Yasser; Favia, Angelo D; Pilka, Ewa S; et al|
|Subject||Alcohol Oxidoreductases Amino Acid Sequence Base Sequence Binding Sites Biocatalysis DNA Primers DNA, Complementary Humans Kinetics Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Sequence Homology, Amino Acid Substrate Specificity chemistry genetics isolation and purification metabolism|