Asparaginase: Difference between revisions
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<StructureSection load='' size='300' side='right' scene='52/525144/ | <StructureSection load='' size='300' side='right' scene='52/525144/Class_ii_3eca/2' caption='First Asparaginase structure (Class_II - [3eca]) dimer, [[3eca]]'> | ||
__TOC__ | __TOC__ | ||
== Function == | == Function == | ||
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'''L-Asparaginases''' are enzymes that hydrolyze the amide group of the amino acid L-asparagine (L-Asn) to L-aspartate, with the simultaneous release of ammonia. They are often referred to as ASNase and assigned the EC number 3.5.1.1; if significant glutaminase co-activity (hydrolysis of the similar amino acid L-glutamine) is also present, the EC number is 3.5.1.38. Some ASNases that belong to other classes (see below) are assigned EC 3.4.19.5. | '''L-Asparaginases''' are enzymes that hydrolyze the amide group of the amino acid L-asparagine (L-Asn) to L-aspartate, with the simultaneous release of ammonia. They are often referred to as ASNase and assigned the EC number 3.5.1.1; if significant glutaminase co-activity (hydrolysis of the similar amino acid L-glutamine) is also present, the EC number is 3.5.1.38. Some ASNases that belong to other classes (see below) are assigned EC 3.4.19.5. | ||
*'''Glycosylasparaginase''' hydrolyzes the bond between asparagine and the sugar moiety in N-linked glycoproteins<ref>PMID:8638940</ref>. | *'''Glycosylasparaginase''' hydrolyzes the bond between asparagine and the sugar moiety in N-linked glycoproteins<ref>PMID:8638940</ref>. | ||
*'''Isoaspartyl peptidase/L-asparaginase''' enables aparaginase and beta-aspartyl-peptidase activity. Invovved in asparagine catabolic process via L-Asp <ref>PMID:15159592</ref>. | |||
== Relevance == | == Relevance == | ||