In most eubacteria, fungi, apicomplexa, plants and some metazoans, the active form of vitamin B6, PLP (pyridoxal 5-phosphate), is de novo synthesized from three substrates, R5P (ribose 5-phosphate), DHAP (dihydroxyacetone phosphate) and ammonia hydrolysed from glutamine by a complexed glutaminase. Of the three active sites of DXP (deoxyxylulose 5-phosphate)independent PLP synthase (Pdx1), the R5P isomerization site has been assigned, but the sites for DHAP isomerization and PLP formation remain unknown. In the present study, we present the crystal structures of yeast Pdx1/Snz1, in apo-, G3P (glyceraldehyde 3-phosphate)- and PLP-bound forms, at 2.3, 1.8 and 2.2 Å (1 Å=0.1 nm) respectively. Structural and biochemical analysis enabled us to assign the PLP-formation site, a G3P-binding site and a G3P-transfer site. We propose a putative catalytic mechanism for Pdx1/Snz1 in which R5P and DHAP are isomerized at two distinct sites and transferred along well-defined routes to a final destination for PLP synthesis.
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Research Article|
November 25 2010
Structural insights into the catalytic mechanism of the yeast pyridoxal 5-phosphate synthase Snz1
Xuan Zhang;
Xuan Zhang
1Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, People's Republic of China
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Yan-Bin Teng;
Yan-Bin Teng
1Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, People's Republic of China
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Jian-Ping Liu;
Jian-Ping Liu
1Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, People's Republic of China
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Yong-Xing He;
Yong-Xing He
1Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, People's Republic of China
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Kang Zhou;
Kang Zhou
1Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, People's Republic of China
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Yuxing Chen;
Yuxing Chen
1Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, People's Republic of China
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Cong-Zhao Zhou
Cong-Zhao Zhou
1
1Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, People's Republic of China
1To whom correspondence should be addressed (email zcz@ustc.edu.cn).
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Publisher: Portland Press Ltd
Received:
August 10 2010
Revision Received:
September 20 2010
Accepted:
October 05 2010
Accepted Manuscript online:
October 05 2010
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2010 Biochemical Society
2010
Biochem J (2010) 432 (3): 445–454.
Article history
Received:
August 10 2010
Revision Received:
September 20 2010
Accepted:
October 05 2010
Accepted Manuscript online:
October 05 2010
Citation
Xuan Zhang, Yan-Bin Teng, Jian-Ping Liu, Yong-Xing He, Kang Zhou, Yuxing Chen, Cong-Zhao Zhou; Structural insights into the catalytic mechanism of the yeast pyridoxal 5-phosphate synthase Snz1. Biochem J 15 December 2010; 432 (3): 445–454. doi: https://doi.org/10.1042/BJ20101241
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