Enzymes
| UniProtKB help_outline | 58,324 proteins |
| Enzyme classes help_outline |
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| GO Molecular Function help_outline |
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- Name help_outline 2-oxoglutarate Identifier CHEBI:16810 (Beilstein: 3664503; CAS: 64-15-3) help_outline Charge -2 Formula C5H4O5 InChIKeyhelp_outline KPGXRSRHYNQIFN-UHFFFAOYSA-L SMILEShelp_outline [O-]C(=O)CCC(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 425 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-leucine Identifier CHEBI:57427 Charge 0 Formula C6H13NO2 InChIKeyhelp_outline ROHFNLRQFUQHCH-YFKPBYRVSA-N SMILEShelp_outline CC(C)C[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 44 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 4-methyl-2-oxopentanoate Identifier CHEBI:17865 (Beilstein: 3904096) help_outline Charge -1 Formula C6H9O3 InChIKeyhelp_outline BKAJNAXTPSGJCU-UHFFFAOYSA-M SMILEShelp_outline CC(C)CC(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 16 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-glutamate Identifier CHEBI:29985 (CAS: 11070-68-1) help_outline Charge -1 Formula C5H8NO4 InChIKeyhelp_outline WHUUTDBJXJRKMK-VKHMYHEASA-M SMILEShelp_outline [NH3+][C@@H](CCC([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 244 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:18321 | RHEA:18322 | RHEA:18323 | RHEA:18324 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Tyrosine aminotransferase: biochemical and structural properties and molecular dynamics simulations.
Mehere P., Han Q., Lemkul J.A., Vavricka C.J., Robinson H., Bevan D.R., Li J.
Tyrosine aminotransferase (TAT) catalyzes the transamination of tyrosine and other aromatic amino acids. The enzyme is thought to play a role in tyrosinemia type II, hepatitis and hepatic carcinoma recovery. The objective of this study is to investigate its biochemical and structural characteristi ... >> More
Tyrosine aminotransferase (TAT) catalyzes the transamination of tyrosine and other aromatic amino acids. The enzyme is thought to play a role in tyrosinemia type II, hepatitis and hepatic carcinoma recovery. The objective of this study is to investigate its biochemical and structural characteristics and substrate specificity in order to provide insight regarding its involvement in these diseases. Mouse TAT (mTAT) was cloned from a mouse cDNA library, and its recombinant protein was produced using Escherichia coli cells and purified using various chromatographic techniques. The recombinant mTAT is able to catalyze the transamination of tyrosine using α-ketoglutaric acid as an amino group acceptor at neutral pH. The enzyme also can use glutamate and phenylalanine as amino group donors and p-hydroxy-phenylpyruvate, phenylpyruvate and alpha-ketocaproic acid as amino group acceptors. Through macromolecular crystallography we have determined the mTAT crystal structure at 2.9 Å resolution. The crystal structure revealed the interaction between the pyridoxal-5'-phosphate cofactor and the enzyme, as well as the formation of a disulphide bond. The detection of disulphide bond provides some rational explanation regarding previously observed TAT inactivation under oxidative conditions and reactivation of the inactive TAT in the presence of a reducing agent. Molecular dynamics simulations using the crystal structures of Trypanosoma cruzi TAT and human TAT provided further insight regarding the substrate-enzyme interactions and substrate specificity. The biochemical and structural properties of TAT and the binding of its cofactor and the substrate may help in elucidation of the mechanism of TAT inhibition and activation. << Less
Protein Cell 1:1023-1032(2010) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Leucine aminotransferase. II. Purification and characterization.
Taylor R.T., Jenkins W.T.
J Biol Chem 241:4396-4405(1966) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Transaminases of branched chain amino acids. IV. Purification and properties of two enzymes from rat liver.
Aki K., Ogawa K., Ichihara A.
Biochim Biophys Acta 159:276-284(1968) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Transamination in Escherichia coli.
Rudman D., Meister A.
J. Biol. Chem. 200:591-604(1953) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Transaminase of branched chain amino acids. VI. Purification and properties of the hog brain enzyme.
Aki K., Yokojima A., Ichihara A.
J Biochem 65:539-544(1969) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Transaminase of branched chain amino acids. I. Branched chain amino acids-alpha-ketoglutarate transaminase.
Ichihara A., Koyama E.
J Biochem 59:160-169(1966) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.