Beaman T W, Binder D A, Blanchard J S, Roderick S L
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
Biochemistry. 1997 Jan 21;36(3):489-94. doi: 10.1021/bi962522q.
The conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA is catalyzed by tetrahydrodipicolinate N-succinyltransferase and is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The X-ray crystal structure of THDP succinyltransferase has been determined to 2.2 A resolution and has been refined to a crystallographic R-factor of 17.0%. The enzyme is trimeric and displays the left-handed parallel beta-helix (L beta H) structural motif encoded by the "hexapeptide repeat" amino acid sequence motif [Raetz, C.R.H., & Roderick, S.L. (1995) Science 270, 997-1000]. The approximate location of the active site of THDP succinyltransferase is suggested by the proximity of binding sites for two inhibitors: p-(chloromercuri)benzenesulfonic acid and cobalt ion, both of which bind to the L beta H domain.
四氢二吡啶甲酸N -琥珀酰转移酶催化四氢二吡啶甲酸和琥珀酰辅酶A转化为N -琥珀酰四氢二吡啶甲酸和辅酶A，这是细菌合成L -赖氨酸和中-二氨基庚二酸（肽聚糖的一个组成成分）的琥珀酰化途径中的关键步骤。已确定四氢二吡啶甲酸琥珀酰转移酶的X射线晶体结构分辨率为2.2埃，并已精修至晶体学R因子为17.0%。该酶是三聚体，呈现由“六肽重复”氨基酸序列基序编码的左手平行β-螺旋（LβH）结构基序[雷茨，C.R.H.，& 罗德里克，S.L.（1995年）《科学》270，997 - 1000]。两种抑制剂：对-（氯汞基）苯磺酸和钴离子的结合位点靠近，提示了四氢二吡啶甲酸琥珀酰转移酶活性位点的大致位置，这两种抑制剂均与LβH结构域结合。
