ENZYMATIC SYNTHESIS OF ANALOGS OF THE CELL-WALL PRECURSOR. I. KINETICS AND SPECIFICITY OF URIDINE DIPHOSPHO-N-ACETYLMURAMYL-L-ALANYL-D-GLUTAMYL-L-LYSINE:D-ALANYL-D-ALANINE LIGASE (ADENOSINE DIPHOSPHATE) FROM STREPTOCOCCUS FAECALIS R.
ENZYMATIC SYNTHESIS OF ANALOGS OF THE CELL-WALL PRECURSOR. I. KINETICS AND SPECIFICITY OF URIDINE DIPHOSPHO-N-ACETYLMURAMYL-L-ALANYL-D-GLUTAMYL-L-LYSINE:D-ALANYL-D-ALANINE LIGASE (ADENOSINE DIPHOSPHATE) FROM STREPTOCOCCUS FAECALIS R.
复制标题
细胞壁前体类似物的酶促合成。
DOI：
10.1021/bi00877a020
复制
发表时间：
1965
期刊：
影响因子：
2.9
通讯作者：
W. Struve
中科院分区：
文献类型：
--
作者：
F. C. Neuhaus;W. Struve
Francis C. Neuhaus and William G. Struve abstract: A specificity profile of the enzyme uridine diphospho-A-) acetylmuramyl-L-alanyl-d-g lutamy 1-l-lysine: D-alanyl-D-alanine ligase (ADP) has been es-tablished. The addition of substituents to the N-terminal residue of the dipeptide enhances the binding of dipeptide in two cases. In contrast, the addi-tion of substituents to the C-terminal residue decreases the binding of the dipeptide in every case. For example, the following pattern is observed (Kmi X 104): Da-amino-n-butyryl-D-alanine (0.9), D-norvalyl-D-alanine (1.2), D-alanyl-D-alanine (1.6), D-alanyl-Da-amino-nbutyryic acid (7.6), D-alanyl-D-norvaline (> 50). The kinetic studies are consistent with a uridine nu-cleotide and dipeptide binding site which are in-dependent of each other. A comparison of the speci-ficity profile of this enzyme with that of D-alanine-D-alanine ligase (ADP) has established a cooperative specificity pattern between two sequential enzyme reactions which are involved in the incorporation of D-alanine into the bacteria] cell-wall precursor, UDP-NAc-muramyl-l-Ala-d-Glu-l-Lys-d-Ala-d-Ala.
