细胞壁脱水胞壁肽循环所需的AmpG通透酶的底物特异性。
Substrate specificity of the AmpG permease required for recycling of cell wall anhydro-muropeptides.
作者信息
Cheng Qiaomei, Park James T
机构信息
Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts 02111, USA.
出版信息
J Bacteriol. 2002 Dec;184(23):6434-6. doi: 10.1128/JB.184.23.6434-6436.2002.
Abstract
AmpG was originally identified as a gene required for induction of beta-lactamase. Subsequently, we found AmpG to be a permease required for recycling of murein tripeptide and uptake of anhydro-muropeptides. We have now studied the specificity of the AmpG permease. The principal requirement is for the presence of the disaccharide, N-acetylglucosaminyl-beta-1,4-anhydro-N-acetylmuramic acid (GlcNAc-anhMurNAc). These unique substrates for AmpG, which contain murein peptides linked to GlcNAc-anhMurNAc, are produced by turnover of the cell wall during logarithmic growth. AmpG permease is sensitive to carbonylcyanide m-chlorophenylhydrazone, demonstrating that AmpG permease is a single-component permease and that transport is dependent on the proton motive force.
摘要
AmpG最初被鉴定为诱导β-内酰胺酶所需的基因。随后，我们发现AmpG是一种通透酶，是胞壁酰三肽循环利用和脱水胞壁肽摄取所必需的。我们现在研究了AmpG通透酶的特异性。主要要求是存在二糖，N-乙酰葡糖胺基-β-1,4-脱水-N-乙酰胞壁酸（GlcNAc-anhMurNAc）。这些AmpG的独特底物含有与GlcNAc-anhMurNAc相连的胞壁肽，是在对数生长期细胞壁周转过程中产生的。AmpG通透酶对羰基氰化物间氯苯腙敏感，表明AmpG通透酶是一种单组分通透酶，且转运依赖于质子动力。
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