(Q27641031)

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Crystal Structure of Thermostable Aspartase from Bacillus sp. YM55-1: Structure-based Exploration of Functional Sites in the Aspartase Family

scientific article (publication date: 2 May 2003)

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scholarly article

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Crystal structure of thermostable aspartase from Bacillus sp. YM55-1: structure-based exploration of functional sites in the aspartase family (English)

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Crystal Structure of Thermostable Aspartase from Bacillus sp. YM55-1: Structure-based Exploration of Functional Sites in the Aspartase Family (English)

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10.1016/S0022-2836(03)00310-3

https://api.crossref.org/works/10.1016/S0022-2836(03)00310-3

26 December 2023

crystal structure

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molecular model

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A12706722

26 December 2023

structural biology

1 reference

10.1016/S0022-2836(03)00310-3

https://api.crossref.org/works/10.1016/S0022-2836(03)00310-3

26 December 2023

author name string

Tomomi Fujii

1

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Hisanobu Sakai

2

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Yasushi Kawata

3

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Yasuo Hata

4

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language of work or name

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publication date

2 May 2003

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full work available at URL

https://api.elsevier.com/content/article/PII:S0022283603003103?httpAccept=text/xml

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10.1016/S0022-2836(03)00310-3

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26 December 2023

https://api.elsevier.com/content/article/PII:S0022283603003103?httpAccept=text/plain

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10.1016/S0022-2836(03)00310-3

https://api.crossref.org/works/10.1016/S0022-2836(03)00310-3

26 December 2023

Journal of Molecular Biology

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328

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3

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635-54

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The structure of L-aspartate ammonia-lyase from Escherichia coli

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7 January 2021

Studies on aspartase. I. Purification and molecular properties of aspartase from Escherichia coli

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7 January 2021

Kinetic studies of L-aspartase from Escherichia coli: pH-dependent activity changes

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7 January 2021

Kinetic studies of L-aspartase from Escherichia coli: substrate activation.

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L-Aspartate-induced activation of aspartase.

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L-aspartate ammonia-lyase and fumarate hydratase share extensive sequence homology.

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Structural and functional relationships between fumarase and aspartase. Nucleotide sequences of the fumarase (fumC) and aspartase (aspA) genes of Escherichia coli K12.

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Evaluation of functionally important amino acids in L-aspartate ammonia-lyase from Escherichia coli.

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Studies on aspartase. II. Role of sulfhydryl groups in aspartase from Escherichia coli

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Chemical modification of essential histidine residues in aspartase with diethylpyrocarbonate

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Assignment of catalytically essential cysteine residues in aspartase by selective chemical modification with N-(7-dimethylamino-4-methylcoumarynyl)maleimide

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Elimination of the sensitivity of L-aspartase to active-site-directed inactivation without alteration of catalytic activity.

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Mapping the mechanism-based modification sites in L-aspartase from Escherichia coli.

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Human argininosuccinate lyase: a structural basis for intragenic complementation

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The structure of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic pathway

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The structure of avian eye lens delta-crystallin reveals a new fold for a superfamily of oligomeric enzymes

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3-Carboxy-cis,cis-muconate lactonizing enzyme from Pseudomonas putida is homologous to the class II fumarase family: a new reaction in the evolution of a mechanistic motif

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7 January 2021

Acid-base chemical mechanism of aspartase from Hafnia alvei

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7 January 2021

Kinetic mechanism and location of rate-determining steps for aspartase from Hafnia alvei

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7 January 2021

Purification and characterization of thermostable aspartase from Bacillus sp. YM55-1.

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Cloning and over-expression of thermostable Bacillus sp. YM55-1 aspartase and site-directed mutagenesis for probing a catalytic residue.

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7 January 2021

Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli

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Mutations of fumarase that distinguish between the active site and a nearby dicarboxylic acid binding site.

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7 January 2021

Chemical mechanism of the endogenous argininosuccinate lyase activity of duck lens delta2-crystallin

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7 January 2021

His68 and His141 are critical contributors to the intersubunit catalytic site of adenylosuccinate lyase of Bacillus subtilis

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Crystal structures of native and recombinant yeast fumarase

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7 January 2021

Crystal structure of an inactive duck delta II crystallin mutant with bound argininosuccinate

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Exploring the role of histidines in the catalytic activity of duck delta-crystallins using site-directed mutagenesis.

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Use of isotope effects to deduce the chemical mechanism of fumarase.

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L-aspartase from Escherichia coli: substrate specificity and role of divalent metal ions.

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The alpha-helix dipole and the properties of proteins

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Structural studies of duck delta 1 and delta 2 crystallin suggest conformational changes occur during catalysis

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Mutational analysis of amino acid residues involved in argininosuccinate lyase activity in duck delta II crystallin

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10.1016/S0022-2836(03)00310-3

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26 December 2023

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