Existence of two D-alanine:D-alanine ligases in Escherichia coli: cloning and sequencing of the ddlA gene and purification and characterization of the DdlA and DdlB enzymes.
作者： Laura E. Zawadzke , Timothy D. H. Bugg , Christopher T. Walsh
DOI: 10.1021/BI00220A033
关键词:
摘要: Two distinct genes encoding D-alanine:D-alanine (D-Ala-D-Ala) ligase (ADP forming) activity in Escherichia coli have been cloned by complementation of E. strain ST640(lambda 112) deficient D-Ala-D-Ala with a lambda library DNA. One the two genes, designated as ddlB, is identical ddl gene already sequenced [Robinson, A.C., Kenan, D.L., Sweeney, J., & Donachie, W.D. (1986) J. Bacteriol. 167, 809-817]. We describe subcloning and DNA sequencing other gene, ddlA on basis similarities Salmonella typhimurium [Daub, E., Zawadzke, L.E., Botstein, D., Walsh, C.T. (1988) Biochemistry 27, 3701-3708]. The predicted amino acid sequence DdlA enzyme shows 90% homology S. sequence. ddlB was subcloned use polymerase chain reaction into an expression vector containing optimized ribosome binding site, which expressed DdlB to greater than 50% soluble cell protein. Both enzymes were purified homogeneity characterized kinetically.
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