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• W2008932846 abstract "Evidence is presented that, in Methanosarcina barkeri oxaloacetate synthesis, an essential and major CO(2) fixation reaction is catalyzed by an apparent alpha(4)beta(4)-type acetyl coenzyme A-independent pyruvate carboxylase (PYC), composed of 64.2-kDa biotinylated and 52.9-kDa ATP-binding subunits. The purified enzyme was most active at 70 degrees C, insensitive to aspartate and glutamate, mildly inhibited by alpha-ketoglutarate, and severely inhibited by ATP, ADP, and excess Mg(2+). It showed negative cooperativity towards bicarbonate at 70 degrees C but not at 37 degrees C. The organism expressed holo-PYC without an external supply of biotin and, thus, synthesized biotin. pycA, pycB, and a putative bpl gene formed a novel operon-like arrangement. Unlike other archaeal homologs, the putative biotin protein ligases (BPLs) of M. barkeri and the closely related euryarchaeon Archaeoglobus fulgidus appeared to be of the Escherichia coli-type (bifunctional, with two activities: BirA or a repressor of the biotin operon and BPL). We found the element Tyr(Phe)ProX(5)Phe(Tyr) to be fully conserved in biotin-dependent enzymes; it might function as the hinge for their swinging arms." @default.
• W2008932846 created "2016-06-24" @default.
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• W2008932846 date "2001-06-15" @default.
• W2008932846 modified "2023-09-25" @default.
• W2008932846 title "Oxaloacetate Synthesis in the Methanarchaeon <i>Methanosarcina barkeri</i> : Pyruvate Carboxylase Genes and a Putative <i>Escherichia coli</i> -Type Bifunctional Biotin Protein Ligase Gene ( <i>bpl/birA</i> ) Exhibit a Unique Organization" @default.
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• W2008932846 doi "https://doi.org/10.1128/jb.183.12.3804-3810.2001" @default.
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