Phosphoserine aminotransferase
From Proteopedia
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<StructureSection load='1w23' size='350' side='right' caption='Phosphoserine aminotransferase dimer complex with pyridoxal phosphate, triethylene glycol, Hepes, Cl- and Mg+2 ions (PDB entry [[1w23]])' scene=''> | <StructureSection load='1w23' size='350' side='right' caption='Phosphoserine aminotransferase dimer complex with pyridoxal phosphate, triethylene glycol, Hepes, Cl- and Mg+2 ions (PDB entry [[1w23]])' scene=''> | ||
== Function == | == Function == | ||
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PSAT is over-expressed in colon tumors and its inhibition is being tested as drug treatment. | PSAT is over-expressed in colon tumors and its inhibition is being tested as drug treatment. | ||
| + | == Structural highlights == | ||
| + | PSAT overall structure shows a small domain and a large one. The active site contains the PLP co-factor bound to lysine side chain<ref>PMID:15608117</ref>. | ||
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| + | </StructureSection> | ||
==3D structures of phosphoserine aminotransferase== | ==3D structures of phosphoserine aminotransferase== | ||
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
Revision as of 10:18, 30 June 2016
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3D structures of phosphoserine aminotransferase
Updated on 30-June-2016
References
- ↑ Basurko MJ, Marche M, Darriet M, Cassaigne A. Phosphoserine aminotransferase, the second step-catalyzing enzyme for serine biosynthesis. IUBMB Life. 1999 Nov;48(5):525-9. PMID:10637769 doi:http://dx.doi.org/10.1080/713803557
- ↑ Dubnovitsky AP, Kapetaniou EG, Papageorgiou AC. Enzyme adaptation to alkaline pH: atomic resolution (1.08 A) structure of phosphoserine aminotransferase from Bacillus alcalophilus. Protein Sci. 2005 Jan;14(1):97-110. PMID:15608117 doi:14/1/97
