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==Human Tyrosine Aminotransferase==
==Human Tyrosine Aminotransferase==
<StructureSection load='3dyd' size='340' side='right' caption='[[3dyd]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3dyd' size='340' side='right'caption='[[3dyd]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3dyd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DYD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DYD FirstGlance]. <br>
<table><tr><td colspan='2'>[[3dyd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DYD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DYD FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TAT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tyrosine_transaminase Tyrosine transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.5 2.6.1.5] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3dyd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dyd OCA], [https://pdbe.org/3dyd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dyd RCSB], [https://www.ebi.ac.uk/pdbsum/3dyd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dyd ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3dyd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dyd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dyd RCSB], [http://www.ebi.ac.uk/pdbsum/3dyd PDBsum]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[http://www.uniprot.org/uniprot/ATTY_HUMAN ATTY_HUMAN]] Defects in TAT are the cause of tyrosinemia type 2 (TYRO2) [MIM:[http://omim.org/entry/276600 276600]]; also known as Richner-Hanhart syndrome. TYRO2 is an inborn error of metabolism characterized by elevations of tyrosine in the blood and urine, and oculocutaneous manifestations. Typical features include palmoplantar keratosis, painful corneal ulcers, and mental retardation.<ref>PMID:1357662</ref>
[https://www.uniprot.org/uniprot/ATTY_HUMAN ATTY_HUMAN] Defects in TAT are the cause of tyrosinemia type 2 (TYRO2) [MIM:[https://omim.org/entry/276600 276600]; also known as Richner-Hanhart syndrome. TYRO2 is an inborn error of metabolism characterized by elevations of tyrosine in the blood and urine, and oculocutaneous manifestations. Typical features include palmoplantar keratosis, painful corneal ulcers, and mental retardation.<ref>PMID:1357662</ref>  
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ATTY_HUMAN ATTY_HUMAN]] Transaminase involved in tyrosine breakdown. Converts tyrosine to p-hydroxyphenylpyruvate. Can catalyze the reverse reaction, using glutamic acid, with 2-oxoglutarate as cosubstrate (in vitro). Has much lower affinity and transaminase activity towards phenylalanine.<ref>PMID:7999802</ref> <ref>PMID:16640556</ref>
[https://www.uniprot.org/uniprot/ATTY_HUMAN ATTY_HUMAN] Transaminase involved in tyrosine breakdown. Converts tyrosine to p-hydroxyphenylpyruvate. Can catalyze the reverse reaction, using glutamic acid, with 2-oxoglutarate as cosubstrate (in vitro). Has much lower affinity and transaminase activity towards phenylalanine.<ref>PMID:7999802</ref> <ref>PMID:16640556</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dy/3dyd_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dy/3dyd_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3dyd ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
==See Also==
*[[Aminotransferase 3D structures|Aminotransferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Tyrosine transaminase]]
[[Category: Large Structures]]
[[Category: Andersson, J]]
[[Category: Andersson J]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith CH]]
[[Category: Berg, S Van Den]]
[[Category: Berglund H]]
[[Category: Berglund, H]]
[[Category: Collins R]]
[[Category: Collins, R]]
[[Category: Dahlgren LG]]
[[Category: Dahlgren, L G]]
[[Category: Edwards AM]]
[[Category: Edwards, A M]]
[[Category: Flodin S]]
[[Category: Flodin, S]]
[[Category: Flores A]]
[[Category: Flores, A]]
[[Category: Graslund S]]
[[Category: Graslund, S]]
[[Category: Hammarstrom M]]
[[Category: Hammarstrom, M]]
[[Category: Johansson A]]
[[Category: Johansson, A]]
[[Category: Johansson I]]
[[Category: Johansson, I]]
[[Category: Karlberg T]]
[[Category: Karlberg, T]]
[[Category: Kotenyova T]]
[[Category: Kotenyova, T]]
[[Category: Lehtio L]]
[[Category: Lehtio, L]]
[[Category: Moche M]]
[[Category: Moche, M]]
[[Category: Nilsson ME]]
[[Category: Nilsson, M E]]
[[Category: Nordlund P]]
[[Category: Nordlund, P]]
[[Category: Nyman T]]
[[Category: Nyman, T]]
[[Category: Olesen K]]
[[Category: Olesen, K]]
[[Category: Persson C]]
[[Category: Persson, C]]
[[Category: Sagemark J]]
[[Category: Structural genomic]]
[[Category: Schuler H]]
[[Category: Sagemark, J]]
[[Category: Thorsell AG]]
[[Category: Schuler, H]]
[[Category: Tresaugues L]]
[[Category: Thorsell, A G]]
[[Category: Van Den Berg S]]
[[Category: Tresaugues, L]]
[[Category: Weigelt J]]
[[Category: Weigelt, J]]
[[Category: Welin M]]
[[Category: Welin, M]]
[[Category: Wikstrom M]]
[[Category: Wikstrom, M]]
[[Category: Wisniewska M]]
[[Category: Wisniewska, M]]
[[Category: Aminotransferase]]
[[Category: Disease mutation]]
[[Category: Phenylalanine catabolism]]
[[Category: Plp]]
[[Category: Pyridoxal phosphate]]
[[Category: Sgc]]
[[Category: Transferase]]
[[Category: Tyrosine]]
[[Category: Tyrosine catabolism]]

Latest revision as of 15:55, 30 August 2023

Human Tyrosine AminotransferaseHuman Tyrosine Aminotransferase

Structural highlights

3dyd is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

ATTY_HUMAN Defects in TAT are the cause of tyrosinemia type 2 (TYRO2) [MIM:276600; also known as Richner-Hanhart syndrome. TYRO2 is an inborn error of metabolism characterized by elevations of tyrosine in the blood and urine, and oculocutaneous manifestations. Typical features include palmoplantar keratosis, painful corneal ulcers, and mental retardation.[1]

Function

ATTY_HUMAN Transaminase involved in tyrosine breakdown. Converts tyrosine to p-hydroxyphenylpyruvate. Can catalyze the reverse reaction, using glutamic acid, with 2-oxoglutarate as cosubstrate (in vitro). Has much lower affinity and transaminase activity towards phenylalanine.[2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Natt E, Kida K, Odievre M, Di Rocco M, Scherer G. Point mutations in the tyrosine aminotransferase gene in tyrosinemia type II. Proc Natl Acad Sci U S A. 1992 Oct 1;89(19):9297-301. PMID:1357662
  2. ↑ Seralini GE, Luu-The V, Labrie F. Cloning and expression of human tyrosine aminotransferase cDNA. Biochim Biophys Acta. 1995 Jan 2;1260(1):97-101. PMID:7999802
  3. ↑ Sivaraman S, Kirsch JF. The narrow substrate specificity of human tyrosine aminotransferase--the enzyme deficient in tyrosinemia type II. FEBS J. 2006 May;273(9):1920-9. PMID:16640556 doi:10.1111/j.1742-4658.2006.05202.x

3dyd, resolution 2.30Å

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