| ID |
899 |
| Name |
Glutathione S-transferase Mu 3 |
| Synonyms |
- EC 2.5.1.18
- GSTM3-3
- GST class-mu 3
- hGSTM3-3
|
| Gene Name |
GSTM3 |
| Protein Sequence |
>Glutathione S-transferase Mu 3
SCESSMVLGYWDIRGLAHAIRLLLEFTDTSYEEKRYTCGEAPDYDRSQWLDVKFKLDLDF
PNLPYLLDGKNKITQSNAILRYIARKHNMCGETEEEKIRVDIIENQVMDFRTQLIRLCYS
SDHEKLKPQYLEELPGQLKQFSMFLGKFSWFAGEKLTFVDFLTYDILDQNRIFDPKCLDE
FPNLKAFMCRFEALEKIAAYLQSDQFCKMPINNKMAQWGNKPVC
|
| Number of Residues |
224 |
| Molecular Weight |
26429 |
| Theoretical pI |
5.19 |
| GO Classification |
| Function |
| catalytic activity |
| transferase activity |
| transferase activity, transferring alkyl or aryl (other than methyl) groups |
| glutathione transferase activity |
| Process |
| physiological process |
| metabolism |
|
| General Function |
Involved in glutathione transferase activity |
| Specific Function |
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May govern uptake and detoxification of both endogenous compounds and xenobiotics at the testis and brain blood barriers |
| Pathways |
Not Available |
| Reactions |
- RX + glutathione = HX + R-S-glutathione
|
| Pfam Domain Function |
|
| Signals |
None |
| Transmembrane Regions |
None |
| Essentiality |
Non-Essential |
| GenBank Protein ID |
306820  |
| UniProtKB ID |
P21266  |
| UniProtKB Entry Name |
GSTM3_HUMAN  |
| PDB ID |
3GTU  |
| PDB File |
show |
| 3D Structure |
View 3D Structure |
| Cellular Location |
Cytoplasm |
| Gene Sequence |
>678 bp
ATGTCGTGCGAGTCGTCTATGGTTCTCGGGTACTGGGATATTCGTGGGCTGGCGCACGCC
ATCCGCCTGCTCCTGGAGTTCACGGATACCTCTTATGAGGAGAAACGGTACACGTGCGGG
GAAGCTCCTGACTATGATCGAAGCCAATGGCTGGATGTGAAATTCAAGCTAGACCTGGAC
TTTCCTAATCTGCCCTACCTCCTGGATGGGAAGAACAAGATCACCCAGAGCAATGCCATC
TTGCGCTACATCGCTCGCAAGCACAACATGTGTGGTGAGACTGAAGAAGAAAAGATTCGA
GTGGACATCATAGAGAACCAAGTAATGGATTTCCGCACACAACTGATAAGGCTCTGTTAC
AGCTCTGACCACGAAAAACTGAAGCCTCAGTACTTGGAAGAGCTACCTGGACAACTGAAA
CAATTCTCCATGTTTCTGTGGAAATTCTCATGGTTTGCCGGGGAAAAGCTCACCTTTGTG
GATTTTCTCACCTATGATATCTTGGATCAGAACCGTATATTTGACCCCAAGTGCCTGGAT
GAGTTCCCAAACCTGAAGGCTTTCATGTGCCGTTTTGAGGCTTTGGAGAAAATCGCTGCC
TACTTACAGTCTGATCAGTTCTGCAAGATGCCCATCAACAACAAGATGGCCCAGTGGGGC
AACAAGCCTGTATGCTGA
|
| GenBank Gene ID |
J05459  |
| GeneCard ID |
GSTM3  |
| GenAtlas ID |
GSTM3  |
| HGNC ID |
HGNC:4635  |
| HPRD ID |
00712 |
| IUPHAR ID |
Not Available |
| Guide to Pharmacology ID |
Not Available |
| Chromosome Location |
Not Available |
| Locus |
1p13.3 |
| SNPs |
GSTM3  |
| General References |
- Campbell E, Takahashi Y, Abramovitz M, Peretz M, Listowsky I: A distinct human testis and brain mu-class glutathione S-transferase. Molecular cloning and characterization of a form present even in individuals lacking hepatic type mu isoenzymes. J Biol Chem. 1990 Jun 5;265(16):9188-93. Pubmed
- Patskovsky YV, Huang MQ, Takayama T, Listowsky I, Pearson WR: Distinctive structure of the human GSTM3 gene-inverted orientation relative to the mu class glutathione transferase gene cluster. Arch Biochem Biophys. 1999 Jan 1;361(1):85-93. Pubmed
- Ross VL, Board PG: Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript. Biochem J. 1993 Sep 1;294 ( Pt 2):373-80. Pubmed
- Hussey AJ, Hayes JD: Human Mu-class glutathione S-transferases present in liver, skeletal muscle and testicular tissue. Biochim Biophys Acta. 1993 Nov 10;1203(1):131-41. Pubmed
- Patskovsky YV, Patskovska LN, Listowsky I: An asparagine-phenylalanine substitution accounts for catalytic differences between hGSTM3-3 and other human class mu glutathione S-transferases. Biochemistry. 1999 Dec 7;38(49):16187-94. Pubmed
|
| Drugs |
| # |
DrugBank ID |
Drug Name |
Drug Type |
Drug Groups |
| 1 |
DB00143 |
Glutathione |
small molecule |
approved, nutraceutical |
| 2 |
DB00163 |
Vitamin E |
small molecule |
approved, nutraceutical |
|