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  1. Article ; Online: Crystallographic and mutational analyses of cystathionine β-synthase in the H

    Matoba, Yasuyuki / Yoshida, Tomoki / Izuhara-Kihara, Hisae / Noda, Masafumi / Sugiyama, Masanori

    Protein science : a publication of the Protein Society

    2017  Volume 26, Issue 4, Page(s) 763–783

    Abstract: Cystathionine β-synthase (CBS) catalyzes the formation of l-cystathionine from l-serine and l-homocysteine. The resulting l-cystathionine is decomposed into l-cysteine, ammonia, and α-ketobutylic acid by cystathionine γ-lyase (CGL). This reverse ... ...

    Abstract Cystathionine β-synthase (CBS) catalyzes the formation of l-cystathionine from l-serine and l-homocysteine. The resulting l-cystathionine is decomposed into l-cysteine, ammonia, and α-ketobutylic acid by cystathionine γ-lyase (CGL). This reverse transsulfuration pathway, which is catalyzed by both enzymes, mainly occurs in eukaryotic cells. The eukaryotic CBS and CGL have recently been recognized as major physiological enzymes for the generation of hydrogen sulfide (H
    MeSH term(s) Amino Acid Substitution ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Binding Sites ; Crystallography, X-Ray ; Cystathionine/metabolism ; Cystathionine beta-Synthase/chemistry ; Cystathionine beta-Synthase/genetics ; Cystathionine beta-Synthase/metabolism ; Hydrogen Sulfide/chemistry ; Hydrogen Sulfide/metabolism ; Hydrolases/genetics ; Hydrolases/metabolism ; Lactobacillus plantarum/enzymology ; Lactobacillus plantarum/genetics ; Multigene Family ; Mutation, Missense
    Chemical Substances Bacterial Proteins ; Cystathionine (375YFJ481O) ; Hydrolases (EC 3.-) ; homocysteinase (EC 3.3.1.-) ; Cystathionine beta-Synthase (EC 4.2.1.22) ; Hydrogen Sulfide (YY9FVM7NSN)
    Language English
    Publishing date 2017-02-10
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1106283-6
    ISSN 1469-896X ; 0961-8368
    ISSN (online) 1469-896X
    ISSN 0961-8368
    DOI 10.1002/pro.3123
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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  2. Article ; Online: Catalytic specificity of the Lactobacillus plantarum cystathionine γ-lyase presumed by the crystallographic analysis.

    Matoba, Yasuyuki / Noda, Masafumi / Yoshida, Tomoki / Oda, Kosuke / Ezumi, Yuka / Yasutake, Chiaki / Izuhara-Kihara, Hisae / Danshiitsoodol, Narandarai / Kumagai, Takanori / Sugiyama, Masanori

    Scientific reports

    2020  Volume 10, Issue 1, Page(s) 14886

    Abstract: The reverse transsulfuration pathway, which is composed of cystathionine β-synthase (CBS) and cystathionine γ-lyase (CGL), plays a role to synthesize L-cysteine using L-serine and the sulfur atom in L-methionine. A plant-derived lactic acid bacterium ... ...

    Abstract The reverse transsulfuration pathway, which is composed of cystathionine β-synthase (CBS) and cystathionine γ-lyase (CGL), plays a role to synthesize L-cysteine using L-serine and the sulfur atom in L-methionine. A plant-derived lactic acid bacterium Lactobacillus plantarum SN35N has been previously found to harbor the gene cluster encoding the CBS- and CGL-like enzymes. In addition, it has been demonstrated that the L. plantarum CBS can synthesize cystathionine from O-acetyl-L-serine and L-homocysteine. The aim of this study is to characterize the enzymatic functions of the L. plantarum CGL. We have found that the enzyme has the high γ-lyase activity toward cystathionine to generate L-cysteine, together with the β-lyase activity toward L-cystine to generate L-cysteine persulfide. By the crystallographic analysis of the inactive CGL K194A mutant complexed with cystathionine, we have found the residues which recognize the distal amino and carboxyl groups of cystathionine or L-cystine. The PLP-bound substrates at the active site may take either the binding pose for the γ- or β-elimination reaction, with the former being the major reaction in the case of cystathionine.
    MeSH term(s) Catalysis ; Crystallography, X-Ray ; Cystathionine/metabolism ; Cystathionine gamma-Lyase/chemistry ; Cystathionine gamma-Lyase/metabolism ; Homocysteine/metabolism ; Lactobacillus plantarum/enzymology ; Serine/analogs & derivatives ; Serine/metabolism ; Substrate Specificity
    Chemical Substances Homocysteine (0LVT1QZ0BA) ; Cystathionine (375YFJ481O) ; Serine (452VLY9402) ; Cystathionine gamma-Lyase (EC 4.4.1.1) ; O-acetylserine (G05L7T7ZEQ)
    Language English
    Publishing date 2020-09-10
    Publishing country England
    Document type Journal Article
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-020-71756-7
    Database MEDical Literature Analysis and Retrieval System OnLINE

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