Journal:Acta Cryst D:S2059798324005461
From Proteopedia
(Difference between revisions)
| Line 8: | Line 8: | ||
==Relevance== | ==Relevance== | ||
| - | Beyond pure academic curiosity, ASNases are also studied because of their potential application as first-line drugs for the treatment of acute lymphoblastic leukemia (ALL)<ref>PMID:27440950</ref><ref>PMID:31552479</ref><ref>PMID:30993718</ref><ref>PMID:31954377</ref>. By clearing L-asparagine from circulation, they starve the L-Asn-dependent malignant cells to death, while sparing the L-Asn-independent healthy cells. The first L-asparaginase introduced for clinical treatment of ALL was Elspar (EcAII from E. coli), followed by Erwinase (ErA from E. chrysanthemi). ASNases are also used in food industry to prevent the formation of acrylamide from L-Asn in fried starch foods<ref>PMID:19388639</ref><ref>PMID:31954377</ref>. | + | Beyond pure academic curiosity, ASNases are also studied because of their potential application as first-line drugs for the treatment of acute lymphoblastic leukemia (ALL)<ref>PMID:27440950</ref><ref>PMID:31552479</ref><ref>PMID:30993718</ref><ref>PMID:31954377</ref>. By clearing L-asparagine from circulation, they starve the L-Asn-dependent malignant cells to death, while sparing the L-Asn-independent healthy cells. The first L-asparaginase introduced for clinical treatment of ALL was Elspar (EcAII from ''E. coli''), followed by Erwinase (ErA from E. chrysanthemi). ASNases are also used in food industry to prevent the formation of acrylamide from L-Asn in fried starch foods<ref>PMID:19388639</ref><ref>PMID:31954377</ref>. |
==Division of ASNases into three classes== | ==Division of ASNases into three classes== | ||
| - | So far, three completely different structural classes of ASNases have been identified<ref>PMID:34258001</ref>, originally named according to the source organism of their isolation<ref>PMID:17143335</ref>, namely Class 1 (bacterial-type), Class 2 (plant-type), and Class 3 (Rhizobium etli-type). This newer classification is intersected with an older convention, which divided the known enzymes with L-asparaginase activity into five types, since in both, Class 1 and Class 3, two types are distinguished according to their compartmentalization and expression profile. The prototypes of types I and II (in Class 1), and III (in Class 2), are the E. coli enzymes EcAI (cytosolic), EcAII (periplasmic), and EcAIII (also cytosolic), respectively. The prototypes of types IV and V (Class 3) are the R. etli enzymes ReAIV (constitutive) and ReAV (inducible). | + | So far, three completely different structural classes of ASNases have been identified<ref>PMID:34258001</ref>, originally named according to the source organism of their isolation<ref>PMID:17143335</ref>, namely Class 1 (bacterial-type), Class 2 (plant-type), and Class 3 (Rhizobium etli-type). This newer classification is intersected with an older convention, which divided the known enzymes with L-asparaginase activity into five types, since in both, Class 1 and Class 3, two types are distinguished according to their compartmentalization and expression profile. The prototypes of types I and II (in Class 1), and III (in Class 2), are the ''E. coli'' enzymes EcAI (cytosolic), EcAII (periplasmic), and EcAIII (also cytosolic), respectively. The prototypes of types IV and V (Class 3) are the R. etli enzymes ReAIV (constitutive) and ReAV (inducible). |
==Dependable Structures== | ==Dependable Structures== | ||
Revision as of 11:18, 11 July 2024
| |||||||||||
Proteopedia Page Contributors and Editors (what is this?)
This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
