Sequence analysis of enzymes with asparaginase activity

Dominika Borek; Mariusz Jaskólski

doi:10.18388/abp.2001_3855

Sequence analysis of enzymes with asparaginase activity

Dominika Borek, Mariusz Jaskólski

Research output: Contribution to journal › Article › peer-review

84 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	893-902
Number of pages	10
Journal	Acta Biochimica Polonica
Volume	48
Issue number	4
DOIs	https://doi.org/10.18388/abp.2001_3855
State	Published - 2001

Keywords

Asparaginase
Aspartylglucosaminidase
L-asparagine
Lysophospholipase
N-terminal nucleophile hydrolase
tRNA amidotransferase

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology

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10.18388/abp.2001_3855

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AU - Jaskólski, Mariusz

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AB - 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.

KW - Asparaginase

KW - Aspartylglucosaminidase

KW - L-asparagine

KW - Lysophospholipase

KW - N-terminal nucleophile hydrolase

KW - tRNA amidotransferase

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JO - Acta Biochimica Polonica

JF - Acta Biochimica Polonica

IS - 4

ER -

Sequence analysis of enzymes with asparaginase activity

Abstract

Keywords

ASJC Scopus subject areas

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