ACS Publications. Most Trusted. Most Cited. Most Read
My Activity

Structure Determination and Characterization of the Vitamin B6 Degradative Enzyme (E)-2-(Acetamidomethylene)succinate Hydrolase,

View Author Information
§ Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853
Department of Chemistry, Texas A&M University, College Station, Texas 77842
*To whom correspondence should be addressed. Telephone: (607) 255-7961. Fax: (607) 255-1227. E-mail: [email protected]; [email protected]
Cite this: Biochemistry 2010, 49, 6, 1226–1235
Publication Date (Web):January 25, 2010
Copyright © 2010 American Chemical Society

    Article Views





    Other access options


    Abstract Image

    The gene identification and kinetic characterization of (E)-2-(acetamidomethylene)succinate (E-2AMS) hydrolase has recently been described. This enzyme catalyzes the final reaction in the degradation of vitamin B6 and produces succinic semialdehyde, acetate, ammonia, and carbon dioxide from E-2AMS. The structure of E-2AMS hydrolase was determined to 2.3 Å using SAD phasing. E-2AMS hydrolase is a member of the α/β hydrolase superfamily and utilizes a serine/histidine/aspartic acid catalytic triad. Mutation of either the nucleophilic serine or the aspartate resulted in inactive enzyme. Mutation of an additional serine residue in the active site causes the enzyme to be unstable and is likely structurally important. The structure also provides insight into the mechanism of hydrolysis of E-2AMS and identifies several potential catalytically important residues.

    Read this article

    To access this article, please review the available access options below.

    Get instant access

    Purchase Access

    Read this article for 48 hours. Check out below using your ACS ID or as a guest.


    Access through Your Institution

    You may have access to this article through your institution.

    Your institution does not have access to this content. You can change your affiliated institution below.

    Cited By

    This article is cited by 13 publications.

    1. Sebastian Fruhauf, Dominic Pühringer, Michaela Thamhesl, Patricia Fajtl, Elisavet Kunz-Vekiru, Andreas Höbartner-Gussl, Gerd Schatzmayr, Gerhard Adam, Jiri Damborsky, Kristina Djinovic-Carugo, Zbynek Prokop, Wulf-Dieter Moll. Bacterial Lactonases ZenA with Noncanonical Structural Features Hydrolyze the Mycotoxin Zearalenone. ACS Catalysis 2024, Article ASAP.
    2. Jessica K. Lukowski, Christopher P. Savas, Alexandra M. Gehring, Magy G. McKary, Chinessa T. Adkins, Luke D. Lavis, Geoffrey C. Hoops, and R. Jeremy Johnson . Distinct Substrate Selectivity of a Metabolic Hydrolase from Mycobacterium tuberculosis. Biochemistry 2014, 53 (47) , 7386-7395.
    3. Bin Liu, Weiwu Wang, Jiguo Qiu, Xing Huang, Shenshen Qiu, Yixuan Bao, Siqiong Xu, Luyao Ruan, Tingting Ran, Jian He. Crystal structures of herbicide-detoxifying esterase reveal a lid loop affecting substrate binding and activity. Nature Communications 2023, 14 (1)
    4. P.B. Mills, E.J. Footitt, P.T. Clayton. Vitamin B6. 2023, 489-503.
    5. Cai You, Fengwei Li, Xingwang Zhang, Li Ma, Yu‐Zhong Zhang, Wei Zhang, Shengying Li. Structural basis for substrate specificity of the peroxisomal acyl‐CoA hydrolase MpaH’ involved in mycophenolic acid biosynthesis. The FEBS Journal 2021, 288 (19) , 5768-5780.
    6. Tianle Qian, Jing Wo, Yan Zhang, Quanwei Song, Guoqiang Feng, Ray Luo, Shuangjin Lin, Geng Wu, Hai-Feng Chen. Crystal Structure of StnA for the Biosynthesis of Antitumor Drug Streptonigrin Reveals a Unique Substrate Binding Mode. Scientific Reports 2017, 7 (1)
    7. Alexis N. Campetelli, Noelia E. Monesterolo. Serine Proteases as Metabolic Regulators in Yeast. 2017, 399-422.
    8. Durairaj Sherlin, Sharmila Anishetty. Mechanistic insights from molecular dynamic simulation of Rv0045c esterase in Mycobacterium tuberculosis. Journal of Molecular Modeling 2015, 21 (4)
    9. Ji-Long Zhang, Qing-Chuan Zheng, Zheng-Qiang Li, Hong-Xing Zhang, . How Does (E)-2-(Acetamidomethylene)succinate Bind to Its Hydrolase? From the Binding Process to the Final Result. PLoS ONE 2013, 8 (1) , e53811.
    10. Tathagata Mukherjee, Jeremiah Hanes, Ivo Tews, Steven E. Ealick, Tadhg P. Begley. Pyridoxal phosphate: Biosynthesis and catabolism. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2011, 1814 (11) , 1585-1596.
    11. Sven Thoms, Julia Hofhuis, Christian Thöing, Jutta Gärtner, Hartmut H. Niemann. The unusual extended C-terminal helix of the peroxisomal α/β-hydrolase Lpx1 is involved in dimer contacts but dispensable for dimerization. Journal of Structural Biology 2011, 175 (3) , 362-371.
    12. Xiangdong Zheng, Jiubiao Guo, Lipeng Xu, Honglei Li, Dongwei Zhang, Kai Zhang, Fei Sun, Tingyi Wen, Siguo Liu, Hai Pang, . Crystal Structure of a Novel Esterase Rv0045c from Mycobacterium tuberculosis. PLoS ONE 2011, 6 (5) , e20506.
    13. Jasleen Bains, Laura Kaufman, Benjamin Farnell, Martin J. Boulanger. A Product Analog Bound Form of 3-Oxoadipate-enol-Lactonase (PcaD) Reveals a Multifunctional Role for the Divergent Cap Domain. Journal of Molecular Biology 2011, 406 (5) , 649-658.

    Pair your accounts.

    Export articles to Mendeley

    Get article recommendations from ACS based on references in your Mendeley library.

    Pair your accounts.

    Export articles to Mendeley

    Get article recommendations from ACS based on references in your Mendeley library.

    You’ve supercharged your research process with ACS and Mendeley!

    STEP 1:
    Click to create an ACS ID

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    Your Mendeley pairing has expired. Please reconnect