Cysteine biosynthesis in the Archaea:: Methanosarcina thermophila utilizes O-acetylserine sulfhydrylase
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作者:
Borup, B
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机构:Penn State Univ, Dept Biochem & Mol Biol, S Frear Lab 205, University Pk, PA 16802 USA
Borup, B
Ferry, JG
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Penn State Univ, Dept Biochem & Mol Biol, S Frear Lab 205, University Pk, PA 16802 USAPenn State Univ, Dept Biochem & Mol Biol, S Frear Lab 205, University Pk, PA 16802 USA
Ferry, JG
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机构:
[1] Penn State Univ, Dept Biochem & Mol Biol, S Frear Lab 205, University Pk, PA 16802 USA
[2] Penn State Univ, Dept Chem, University Pk, PA 16802 USA
Two pathways for cysteine biosynthesis are known in nature; however, it is not known which, if either, the Archaea utilize. Enzyme activities in extracts of Methanosarcina thermophila grown with combinations of cysteine and sulfide as sulfur sources indicated that this archaeon utilizes the pathway found in the Bacteria domain. The genes encoding serine transacetylase and O-acetylserine sulfhydrylase (cysE and cysK) are adjacent on the chromosome of M. thermophila and possibly form an operon. When M. thermophila is grown with cysteine as the sole sulfur source, O-acetylserine sulfhydrylase activity is maximally expressed suggesting alternative roles for this enzyme apart from cysteine biosynthesis. (C) 2000 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
机构:
Virginia Commonwealth Univ, Dept Med Chem, Richmond, VA 23298 USA
Virginia Commonwealth Univ, Inst Struct Biol & Drug Design, Richmond, VA 23298 USAUniv Parma, Dept Biochem & Mol Biol, I-43100 Parma, Italy
机构:
Virginia Commonwealth Univ, Dept Med Chem, Richmond, VA 23298 USA
Virginia Commonwealth Univ, Inst Struct Biol & Drug Design, Richmond, VA 23298 USAUniv Parma, Dept Biochem & Mol Biol, I-43100 Parma, Italy