Articles with "argininosuccinate lyase" as a keyword



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Biochemical characterization of argininosuccinate lyase from M. tuberculosis: significance of a cā€terminal cysteine in catalysis and thermal stability

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Published in 2017 at "IUBMB Life"

DOI: 10.1002/iub.1683

Abstract: Arginine biosynthesis pathway is crucial to the survival and pathogenesis of Mycobacterium tuberculosis (Mtb). Arginine is a critical amino acid that contributes to the inflection of cellular immune responses during pathogenesis. Argininosuccinate lyase from Mtb… read more here.

Keywords: cysteine; cys441; tuberculosis; activity ... See more keywords
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Structural studies on M. tuberculosis argininosuccinate lyase and its liganded complex: Insights into catalytic mechanism

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Published in 2019 at "IUBMB Life"

DOI: 10.1002/iub.2000

Abstract: Argininosuccinate lyase catalyses the reversible breakdown of argininosuccinate into arginine and fumarate and is known to form tetramers in its quaternary association. The absence of structures involving competent enzymes bound to substrate/products came in the… read more here.

Keywords: studies tuberculosis; mechanism; catalytic mechanism; structural studies ... See more keywords
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Low prevalence of argininosuccinate lyase deficiency among inherited urea cycle disorders in Korea

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Published in 2018 at "Journal of Human Genetics"

DOI: 10.1038/s10038-018-0467-2

Abstract: Argininosuccinic aciduria (ASA), which is considered to be the second most common urea cycle disorder (UCD), is caused by an argininosuccinate lyase deficiency and is biochemically characterized by elevation of argininosuccinic acid and arginine deficiency.… read more here.

Keywords: prevalence; lyase deficiency; urea cycle; deficiency ... See more keywords
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Structural studies on M. tuberculosis argininosuccinate lyase and its liganded complex: Insights into catalytic mechanism.

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Published in 2019 at "Iubmb Life"

DOI: 10.2210/pdb6iem/pdb

Abstract: Argininosuccinate lyase catalyses the reversible breakdown of argininosuccinate into arginine and fumarate and is known to form tetramers in its quaternary association. The absence of structures involving competent enzymes bound to substrate/products came in the… read more here.

Keywords: argininosuccinate lyase; structural studies; studies tuberculosis; mechanism ... See more keywords