Domain architecture of pyruvate carboxylase, a biotin-dependent multifunctional enzyme (Q27647506)

7

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author name string

Martin St Maurice

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Laurie Reinhardt

2

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Kathy H Surinya

3

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Paul V Attwood

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John C Wallace

5

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W Wallace Cleland

Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions

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language of work or name

English

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publication date

24 August 2007

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published in

Science

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volume

317

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issue

5841

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page(s)

1076-9

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cites work

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Acetyl-coenzyme A carboxylase: crucial metabolic enzyme and attractive target for drug discovery

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Solution structures of apo and holo biotinyl domains from acetyl coenzyme A carboxylase of Escherichia coli determined by triple-resonance nuclear magnetic resonance spectroscopy

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Crystal structure of the carboxyltransferase domain of the oxaloacetate decarboxylase Na+ pump from Vibrio cholerae

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Movement of the biotin carboxylase B-domain as a result of ATP binding

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Carbamoyl phosphate synthetase: closure of the B-domain as a result of nucleotide binding

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Molecular structure of Escherichia coli PurT-encoded glycinamide ribonucleotide transformylase

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Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions

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Domains, motifs, and linkers in 2-oxo acid dehydrogenase multienzyme complexes: a paradigm in the design of a multifunctional protein

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Enzymes with molecular tunnels

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The biotin enzyme family: conserved structural motifs and domain rearrangements

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Anaplerotic roles of pyruvate carboxylase in mammalian tissues

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Structure of the biotin carboxylase subunit of pyruvate carboxylase from Aquifex aeolicus at 2.2 A resolution

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Transcarboxylase 5S structures: assembly and catalytic mechanism of a multienzyme complex subunit

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Chemical and catalytic mechanisms of carboxyl transfer reactions in biotin-dependent enzymes

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Identification of the catalytic residues involved in the carboxyl transfer of pyruvate carboxylase.

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The existence of multiple tetrameric conformers of chicken liver pyruvate carboxylase and their roles in dilution inactivation

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Fatty acid synthase dimers containing catalytically active beta-ketoacyl synthase or malonyl/acetyltransferase domains in only one subunit can support fatty acid synthesis at the acyl carrier protein domains of both subunits

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The 2.7-Angstrom crystal structure of a 194-kDa homodimeric fragment of the 6-deoxyerythronolide B synthase.

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Further studies on the localization of the reactive lysyl residue of pyruvate carboxylase

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Modeling and numerical simulation of biotin carboxylase kinetics: implications for half-sites reactivity.

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Identification of lysine-238 of Escherichia coli biotin carboxylase as an ATP-binding residue.

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Identifiers

DOI

10.1126/SCIENCE.1144504

1 reference

Consolidated OpenCitations Corpus – April 2017

2345876

2345876

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference