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A retro-evolution study of CDP-6-deoxy-D-glycero-L-threo-4-hexulose-3-dehydrase (E1) from Yersinia pseudotuberculosis: implications for C-3 deoxygenation in the biosynthesis of 3,6-dideoxyhexoses.
Biochemistry. 2007 Mar 27; 46(12):3759-67.B

Abstract

CDP-6-deoxy-l-threo-d-glycero-4-hexulose-3-dehydrase (E1), which catalyzes C-3 deoxygenation of CDP-4-keto-6-deoxyglucose in the biosynthesis of 3,6-dideoxyhexoses, shares a modest sequence identity with other B6-dependent enzymes, albeit with two important distinctions. It is a rare example of a B6-dependent enzyme that harbors a [2Fe-2S] cluster, and a highly conserved lysine that serves as an anchor for PLP in most B6-dependent enzymes is replaced by histidine at position 220 in E1. Since alteration of His220 to a lysine residue may produce a putative progenitor of E1, the H220K mutant was constructed and tested for the ability to process the predicted substrate, CDP-4-amino-4,6-dideoxyglucose, using PLP as the coenzyme. Our data showed that H220K-E1 has no dehydrase activity, but can act as a PLP-dependent transaminase. However, the reaction is not catalytic since PLP cannot be regenerated during turnover. Reported herein are the results of this investigation and the implications for the role of His220 in the catalytic mechanism of E1.

Authors+Show Affiliations

Division of Medicinal Chemistry, College of Pharmacy, and Department of Chemistry and Biochemistry, University of Texas, Austin, Texas 78712, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural

Language

eng

PubMed ID

17323931

Citation

Wu, Qingquan, et al. "A Retro-evolution Study of CDP-6-deoxy-D-glycero-L-threo-4-hexulose-3-dehydrase (E1) From Yersinia Pseudotuberculosis: Implications for C-3 Deoxygenation in the Biosynthesis of 3,6-dideoxyhexoses." Biochemistry, vol. 46, no. 12, 2007, pp. 3759-67.
Wu Q, Liu YN, Chen H, et al. A retro-evolution study of CDP-6-deoxy-D-glycero-L-threo-4-hexulose-3-dehydrase (E1) from Yersinia pseudotuberculosis: implications for C-3 deoxygenation in the biosynthesis of 3,6-dideoxyhexoses. Biochemistry. 2007;46(12):3759-67.
Wu, Q., Liu, Y. N., Chen, H., Molitor, E. J., & Liu, H. W. (2007). A retro-evolution study of CDP-6-deoxy-D-glycero-L-threo-4-hexulose-3-dehydrase (E1) from Yersinia pseudotuberculosis: implications for C-3 deoxygenation in the biosynthesis of 3,6-dideoxyhexoses. Biochemistry, 46(12), 3759-67.
Wu Q, et al. A Retro-evolution Study of CDP-6-deoxy-D-glycero-L-threo-4-hexulose-3-dehydrase (E1) From Yersinia Pseudotuberculosis: Implications for C-3 Deoxygenation in the Biosynthesis of 3,6-dideoxyhexoses. Biochemistry. 2007 Mar 27;46(12):3759-67. PubMed PMID: 17323931.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A retro-evolution study of CDP-6-deoxy-D-glycero-L-threo-4-hexulose-3-dehydrase (E1) from Yersinia pseudotuberculosis: implications for C-3 deoxygenation in the biosynthesis of 3,6-dideoxyhexoses. AU - Wu,Qingquan, AU - Liu,Yung-Nan, AU - Chen,Huawei, AU - Molitor,Erich J, AU - Liu,Hung-wen, Y1 - 2007/02/27/ PY - 2007/2/28/pubmed PY - 2007/5/10/medline PY - 2007/2/28/entrez SP - 3759 EP - 67 JF - Biochemistry JO - Biochemistry VL - 46 IS - 12 N2 - CDP-6-deoxy-l-threo-d-glycero-4-hexulose-3-dehydrase (E1), which catalyzes C-3 deoxygenation of CDP-4-keto-6-deoxyglucose in the biosynthesis of 3,6-dideoxyhexoses, shares a modest sequence identity with other B6-dependent enzymes, albeit with two important distinctions. It is a rare example of a B6-dependent enzyme that harbors a [2Fe-2S] cluster, and a highly conserved lysine that serves as an anchor for PLP in most B6-dependent enzymes is replaced by histidine at position 220 in E1. Since alteration of His220 to a lysine residue may produce a putative progenitor of E1, the H220K mutant was constructed and tested for the ability to process the predicted substrate, CDP-4-amino-4,6-dideoxyglucose, using PLP as the coenzyme. Our data showed that H220K-E1 has no dehydrase activity, but can act as a PLP-dependent transaminase. However, the reaction is not catalytic since PLP cannot be regenerated during turnover. Reported herein are the results of this investigation and the implications for the role of His220 in the catalytic mechanism of E1. SN - 0006-2960 UR - https://www.unboundmedicine.com/medline/citation/17323931/A_retro_evolution_study_of_CDP_6_deoxy_D_glycero_L_threo_4_hexulose_3_dehydrase__E1__from_Yersinia_pseudotuberculosis:_implications_for_C_3_deoxygenation_in_the_biosynthesis_of_36_dideoxyhexoses_ L2 - https://doi.org/10.1021/bi602352g DB - PRIME DP - Unbound Medicine ER -