Momany C, Ghosh R, Hackert M L
Department of Chemistry and Biochemistry, University of Texas at Austin 78712, USA.
Protein Sci. 1995 May;4(5):849-54. doi: 10.1002/pro.5560040504.
Two of the five domains in the structure of the ornithine decarboxylase (OrnDC) from Lactobacillus 30a share similar structural folds around the pyridoxal-5'-phosphate (PLP)-binding pocket with the aspartate aminotransferases (AspATs). Sequence comparisons focusing on conserved residues of the aligned structures reveal that this structural motif is also present in a number of other PLP-dependent enzymes including the histidine, dopa, tryptophan, glutamate, and glycine decarboxylases as well as tryptophanase and serine-hydroxymethyl transferase. However, this motif is not present in eukaryotic OrnDCs, the diaminopimelate decarboxylases, nor the Escherichia coli or oat arginine decarboxylases. The identification and comparison of residues involved in defining the different classes are discussed.
来自乳酸杆菌30a的鸟氨酸脱羧酶（OrnDC）结构中的五个结构域中有两个，在磷酸吡哆醛（PLP）结合口袋周围与天冬氨酸转氨酶（AspATs）具有相似的结构折叠。聚焦于比对结构保守残基的序列比较表明，这种结构基序也存在于许多其他依赖PLP的酶中，包括组氨酸、多巴、色氨酸、谷氨酸和甘氨酸脱羧酶，以及色氨酸酶和丝氨酸羟甲基转移酶。然而，这种基序在真核生物的OrnDC、二氨基庚二酸脱羧酶、大肠杆菌或燕麦精氨酸脱羧酶中不存在。文中讨论了参与定义不同类别残基的鉴定和比较。
