Structural aspects of L-asparaginases, their friends and relations
Structural aspects of L-asparaginases, their friends and relations
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DOI：
10.18388/abp.2006_3291
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发表时间：
2006-01-01
影响因子：
1.7
通讯作者：
Jaskolski, Mariusz
中科院分区：
文献类型：
--
作者：
Michalska, Karohna;Jaskolski, Mariusz
Enzymes capable of converting L-asparagine to L-aspartate can be classified as bacterial-type or plant-type L-asparaginases. Bacterial-type L-asparaginases are further divided into subtypes I and II, defined by their intra-/extra-cellular localization, substrate affinity, and oligomeric form. Plant-type L-asparaginases are evolutionarily and structurally distinct from the bacterial-type enzymes. They function as potassium-dependent or -independent Ntn-hydrolases, similar to the well characterized aspartylglucosaminidases with (alpha beta)(2) oligomeric structure. The review discusses the structural aspects of both types of L-asparaginases and highlights some peculiarities of their catalytic mechanisms. The bacterial-type enzymes are believed to have a disordered active site which gets properly organized on substrate binding. The plant-type enzymes, which are more active as isoaspartyl aminopeptidases, pose a chemical challenge common to other Ntn-hydrolases, which is how an N-terminal nucleophile can activate itself or cleave its own a-amide bond before the activation is even possible. The K+-independent plant-type L-asparaginases show an unusual sodium coordination by main-chain carbonyl groups and have a key arginine residue which by sensing the arrangement at the oligomeric (alpha beta)-(alpha beta) interface is able to discriminate among substrates presented for hydrolysis.
