3dyd
From Proteopedia
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{{STRUCTURE_3dyd| PDB=3dyd | SCENE= }} | {{STRUCTURE_3dyd| PDB=3dyd | SCENE= }} | ||
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===Human Tyrosine Aminotransferase=== | ===Human Tyrosine Aminotransferase=== | ||
+ | ==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> | ||
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+ | ==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> | ||
==About this Structure== | ==About this Structure== | ||
[[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]. | [[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]. | ||
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+ | ==Reference== | ||
+ | <references group="xtra"/><references/> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Tyrosine transaminase]] | [[Category: Tyrosine transaminase]] |
Revision as of 01:55, 25 March 2013
Contents |
Human Tyrosine Aminotransferase
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]
About this Structure
3dyd is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- ↑ 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
- ↑ 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
- ↑ 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
Categories: Homo sapiens | Tyrosine transaminase | Andersson, J. | Arrowsmith, C H. | Berg, S Van Den. | Berglund, H. | Collins, R. | Dahlgren, L G. | Edwards, A M. | Flodin, S. | Flores, A. | Graslund, S. | Hammarstrom, M. | Johansson, A. | Johansson, I. | Karlberg, T. | Kotenyova, T. | Lehtio, L. | Moche, M. | Nilsson, M E. | Nordlund, P. | Nyman, T. | Olesen, K. | Persson, C. | SGC, Structural Genomics Consortium. | Sagemark, J. | Schuler, H. | Thorsell, A G. | Tresaugues, L. | Weigelt, J. | Welin, M. | Wikstrom, M. | Wisniewska, M. | Aminotransferase | Disease mutation | Phenylalanine catabolism | Plp | Pyridoxal phosphate | Sgc | Structural genomic | Structural genomics consortium | Transferase | Tyrosine | Tyrosine catabolism