دورية أكاديمية
Identification of coenzyme M biosynthetic 2-phosphosulfolactate phosphatase. A member of a new class of Mg(2+)-dependent acid phosphatases.
| العنوان: | Identification of coenzyme M biosynthetic 2-phosphosulfolactate phosphatase. A member of a new class of Mg(2+)-dependent acid phosphatases. |
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| المؤلفون: | Graham DE; Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061, USA., Graupner M, Xu H, White RH |
| المصدر: | European journal of biochemistry [Eur J Biochem] 2001 Oct; Vol. 268 (19), pp. 5176-88. |
| نوع المنشور: | Journal Article; Research Support, U.S. Gov't, Non-P.H.S. |
| اللغة: | English |
| بيانات الدورية: | Publisher: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID: 0107600 Publication Model: Print Cited Medium: Print ISSN: 0014-2956 (Print) Linking ISSN: 00142956 NLM ISO Abbreviation: Eur J Biochem Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: -2004: Oxford, UK : Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Original Publication: Berlin, New York, Springer. |
| مواضيع طبية MeSH: | Acid Phosphatase/*biosynthesis , Mesna/*metabolism , Methanococcus/*enzymology, Acid Phosphatase/chemistry ; Acid Phosphatase/metabolism ; Amino Acid Sequence ; Base Sequence ; DNA Primers ; Hydrolysis ; Kinetics ; Molecular Sequence Data ; Phylogeny ; Sequence Homology, Amino Acid ; Stereoisomerism ; Substrate Specificity |
| مستخلص: | Coenzyme M (CoM; 2-mercaptoethanesulfonic acid) is the terminal methyl carrier in methanogenesis. Methanogenic archaea begin the production of this essential cofactor by sulfonating phosphoenolpyruvate to form 2-phospho-3-sulfolactate. After dephosphorylation, this precursor is oxidized, decarboxylated and then reductively thiolated to form CoM. A thermostable phosphosulfolactate phosphohydrolase (EC 3.1.3.-) catalyzing the second step in CoM biosynthesis, was identified in the hyperthermophilic euryarchaeon Methanococcus jannaschii. The predicted ORF MJ1140 in the genome of M. jannaschii encodes ComB, a Mg2+-dependent acid phosphatase that is specific for 2-hydroxycarboxylic acid phosphate esters. Recombinantly expressed purified ComB efficiently hydrolyzes rac-2-phosphosulfolactate, (S)-2-phospholactate, phosphoglycolate and both enantiomers of 2-phosphomalate. In contrast to previously studied phosphoglycolate phosphatases, ComB has a low pH optimum for activity, a narrow substrate specificity and an amino acid sequence dissimilar to any biochemically characterized protein. Like other phosphatases that function via covalent phosphoenzyme intermediates, ComB can catalyze a transphosphorylation reaction. Homologs of comB are identified in all available cyanobacterial genome sequences and in genomes from phylogenetically diverse bacteria and archaea; most of these organisms lack homologs of other CoM biosynthetic genes. The broad and disparate distribution of comB homologs suggests that the gene has been recruited frequently into new metabolic pathways. |
| المشرفين على المادة: | 0 (DNA Primers) EC 3.1.3.2 (Acid Phosphatase) EC 3.1.3.71 (2-phosphosulfolactate phosphatase) NR7O1405Q9 (Mesna) |
| تواريخ الأحداث: | Date Created: 20011009 Date Completed: 20011204 Latest Revision: 20190620 |
| رمز التحديث: | 20221213 |
| DOI: | 10.1046/j.0014-2956.2001.02451.x |
| PMID: | 11589710 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 0014-2956 |
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| DOI: | 10.1046/j.0014-2956.2001.02451.x |