3dyd

Human Tyrosine AminotransferaseHuman Tyrosine Aminotransferase

Structural highlights

3dyd is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	TAT (HUMAN)
Activity:	Tyrosine transaminase, with EC number 2.6.1.5
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.

References

↑ 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

[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

[1]

[2]

[3]

3dyd

Human Tyrosine AminotransferaseHuman Tyrosine Aminotransferase

Structural highlights

Disease

Function

Evolutionary Conservation

References

Contents

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

3dyd

Human Tyrosine AminotransferaseHuman Tyrosine Aminotransferase

Structural highlights

Disease

Function

Evolutionary Conservation

References

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Search