4“-phosphopantothenoylcysteine合成酶的分子特征域的细菌dfp黄素蛋白。
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Kupke T
4“-phosphopantothenoylcysteine合成酶的分子特征域的细菌dfp黄素蛋白。
J生物化学杂志。2002年9月27日,277 (39):36137 - 45。Epub 2002年7月24日。
- PubMed ID
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12140293 (在PubMed]
- 文摘
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在细菌中,辅酶A合成泛酸盐的五个步骤。黄素蛋白的Dfp催化辅酶A的合成前体4的存在4中-phosphopantetheine -phosphopantothenate,半胱氨酸、CTP、镁(2 +)(施特劳斯,E。Kinsland C。通用电气,Y。、McLafferty f·W。贝格利,t p(2001)生物。276年化学,13513 - 13516)。已经表明,NH(2)终端域Dfp有4个-phosphopantothenoylcysteine脱羧酶的活动(Kupke, T。Uebele, M。施密德,D。荣格,G。Blaesse, M。罗伯塔,s(2000)生物。275年化学,31838 - 31846)。我证明COOH-terminal CoaB Dfp催化领域的合成4 -phosphopantothenoylcysteine。 The exchange of conserved amino acid residues within the CoaB domain revealed that the synthesis of 4'-phosphopantothenoylcysteine occurs in two half-reactions. Using the mutant protein His-CoaB N210D the putative acyl-cytidylate intermediate of 4'-phosphopantothenate was detectable. The same intermediate was detectable for the wild-type CoaB enzyme if cysteine was omitted in the reaction mixture. Exchange of the conserved Lys(289) residue, which is part of the strictly conserved (289)KXKK(292) motif of the CoaB domain, resulted in complete loss of activity with neither the acyl-cytidylate intermediate nor 4'-phosphopantothenoylcysteine being detectable. Gel filtration experiments indicated that CoaB forms dimers. Residues that are important for dimerization are conserved in CoaB proteins from eubacteria, Archaea, and eukaryotes.