Description

IPR040077 is a Glutathione S-transferase Theta, C-terminal.

<p>This entry represents the C-terminal domain found in class Theta GSTs. Proteins containing this domain also include bacterial dichloromethane (DCM) dehalogenase.</p> <p>GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. Cytosolic GSTs from mammals can be divided into four distinct classes: Alpha, Mu, Pi and Theta. The GST fold contains an N-terminal TRX-fold domain and a C-terminal α helical domain, with an active site located in a cleft between the two domains [[cite:PUB00090504], [cite:PUB00023114]].</p> <p>Mammalian class Theta GSTs show poor GSH conjugating activity towards the standard substrates, CDNB and ethacrynic acid, differentiating them from other mammalian GSTs [[cite:PUB00090505], [cite:PUB00090506]]. GSTT1-1 shows similar cataytic activity as bacterial DCM dehalogenase, catalyzing the GSH-dependent hydrolytic dehalogenation of dihalomethanes. This is an essential process in methylotrophic bacteria to enable them to use chloromethane and DCM as sole carbon and energy sources. The presence of polymorphisms in human GSTT1-1 and its relationship to the onset of diseases including cancer is subject of many studies [[cite:PUB00039877], [cite:PUB00090507]]. Human GSTT2-2 exhibits a highly specific sulfatase activity, catalyzing the cleavage of sulfate ions from aralkyl sufate esters, but not from aryl or alkyl sulfate esters [[cite:PUB00090508]].</p>

This description is obtained from EB-eye REST.

Associated GO terms

Unable to find any GO terms for the transcript with the identifier.

Associated Lotus transcripts 3

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: