Abstrakt

Aminotransferaza asparaginianowa (AST) jest enzymem nieswoistym narządowo, występującym w wielu tkankach organizmu człowieka, gdzie katalizuje odwracalną reakcję transaminacji. Istnieją dwie izoformy aminotransferazy asparaginianowej – cytoplazmatyczna (AST1) i mitochondrialna (AST2), które zwykle występują razem i współdziałają metabolicznie. Obie izoformy są homodimerami z wysoce konserwatywnymi regionami odpowiedzialnymi za katalityczne właściwości enzymu. Cechą wspólną wszystkich znanych aminotransferaz asparaginianowych jest konserwatywna reszta Lys-259, która tworzy wiązanie kowalencyjne z grupą prostetyczną – fosforanem pirydoksalu. Różnice w budowie pierwszorzędowej obu izoform determinują ich odmienne właściwości fizykochemiczne, kinetyczne i immunologiczne. Z powodu niskiego stężenia L-asparaginianu (L-Asp) we krwi, aminotransferaza asparaginianowa jest jedynym enzymem dostarczającym ten aminokwas jako substrat do wielu procesów metabolicznych, takich jak cykl mocznikowy oraz synteza nukleotydów purynowych i pirymidynowych w wątrobie, synteza L-argininy w nerkach oraz cykl nukleotydów purynowych w mózgu i mięśniach szkieletowych. AST uczestniczy także w powstawaniu D-asparaginianu, który reguluje metabolizm na poziomie auto-, para- i endokrynnym. Aminotransferaza asparaginianowa wchodzi w skład czółenka jabłczanowo-asparaginianowego w mięśniu sercowym, bierze udział w procesach glukoneogenezy w wątrobie i nerce, gliceroneogenezy w tkance tłuszczowej oraz syntezie neuroprzekaźników w szlaku neuronowo-glejowym mózgu. W ostatnich latach stwierdzono istotny udział aminotransferazy asparaginianowej w glutaminolizie – podstawowym szlaku metabolicznym w komórkach nowotworowych.W artykule omówiono rolę AST, znanej głównie jako enzym diagnostyczny chorób wątroby,w przemianach metabolicznych różnych tkanek i narządów organizmu człowieka.

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