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    Wyświetlanie 1-3 z 3
    Tytuł:
    Sequence analysis of enzymes with asparaginase activity.
    Autorzy:
    Borek, Dominika
    Jaskólski, Mariusz
    Powiązania:
    https://bibliotekanauki.pl/articles/1044033.pdf
    Data publikacji:
    2001
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    N-terminal nucleophile hydrolase
    lysophospholipase
    tRNA amidotransferase
    aspartylglucosaminidase
    asparaginase
    L-asparagine
    Opis:
    Asparaginases catalyze the hydrolysis of asparagine to aspartic acid and ammonia. Enzymes with asparaginase activity play an important role both in the metabolism of all living organisms as well as in pharmacology. The main goal of this paper is to attempt a classification of all known enzymes with asparaginase activity, based on their amino acid sequences. Some possible phylogenetic consequences are also discussed using dendrograms and structural information derived from crystallographic studies.
    Źródło:
    Acta Biochimica Polonica; 2001, 48, 4; 893-902
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Structural aspects of l-asparaginases, their friends and relations
    Autorzy:
    Michalska, Karolina
    Jaskolski, Mariusz
    Powiązania:
    https://bibliotekanauki.pl/articles/1041150.pdf
    Data publikacji:
    2006
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    Ntn-hydrolase
    l-asparaginase
    isoaspartyl peptidase
    Opis:
    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 (αβ)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 α-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 (αβ)-(αβ) interface is able to discriminate among substrates presented for hydrolysis.
    Źródło:
    Acta Biochimica Polonica; 2006, 53, 4; 627-640
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    L-asparaginase: An ultimate anti-neoplastic enzyme
    Autorzy:
    Prasad Talluri, V.S.S.L.
    Bhavana, M.
    Mahesh Kumar, M.V.S.
    Rajagopal, S.V.
    Powiązania:
    https://bibliotekanauki.pl/articles/11250.pdf
    Data publikacji:
    2014
    Wydawca:
    Przedsiębiorstwo Wydawnictw Naukowych Darwin / Scientific Publishing House DARWIN
    Tematy:
    L-asparaginase
    anti-neoplastic enzyme
    enzyme
    acute lymphoblastic leukemia
    chemotherapeutic drug
    Opis:
    The objective of the study described the importance of L-asparaginase and its importance in the field of medicine. Different types of enzymes are produced based on the adaptation to the environment where the living organisms live to tune the metabolic pathways according to their adapted changes. The enzymes present in various organs are produced by many cell types in multicellular organisms. Except ribosomes all other known enzymes are proteinaceous in nature. L-asparaginase is a potential therapeutic agent for acute lymphoblastic leukemia (ALL) and chronic myelogenous leukemia which is approved by FDA & WHO. L-asparaginase catalyzes the deamination of L-asparagine to L-aspartic acid & ammonia. Unlike normal cells, malignant cells require large amount of L-asparagine for protein synthesis and cell division. From this background the present review is an effort to gather the information on the mechanism, sources, molecular details and application of L-asparaginase enzyme.
    Źródło:
    International Letters of Natural Sciences; 2014, 10
    2300-9675
    Pojawia się w:
    International Letters of Natural Sciences
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-3 z 3

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