Mechanistic characterization of the MSDH (methylmalonate semialdehyde dehydrogenase) from Bacillus subtilis (Q24541310)

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Language	Label	Description	Also known as
English	Mechanistic characterization of the MSDH (methylmalonate semialdehyde dehydrogenase) from Bacillus subtilis	scientific article

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instance of

scholarly article

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title

Mechanistic characterization of the MSDH (methylmalonate semialdehyde dehydrogenase) from Bacillus subtilis (English)

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main subject

cell biology

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Bacillus subtilis

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based on heuristic

inferred from title

author name string

Claire Stines-Chaumeil

series ordinal

1

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François Talfournier

series ordinal

2

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Guy Branlant

series ordinal

3

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language of work or name

English

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publication date

1 April 2006

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published in

Biochemical Journal

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volume

395

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issue

1

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page(s)

107-15

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cites work

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Apo and holo crystal structures of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans

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The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold

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Characterization of the mmsAB operon of Pseudomonas aeruginosa PAO encoding methylmalonate-semialdehyde dehydrogenase and 3-hydroxyisobutyrate dehydrogenase

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Expression, purification, crystallization and preliminary X-ray diffraction data of methylmalonate-semialdehyde dehydrogenase from Bacillus subtilis.

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PduP is a coenzyme-a-acylating propionaldehyde dehydrogenase associated with the polyhedral bodies involved in B 12 -dependent 1,2-propanediol degradation by Salmonella enterica serovar Typhimurium LT2

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Role of glutamate-268 in the catalytic mechanism of nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans

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Evidence for the chemical activation of essential cys-302 upon cofactor binding to nonphosphorylating glyceraldehyde 3-phosphate dehydrogenase from Streptococcus mutans

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Basis for half-of-the-site reactivity and the dominance of the K487 oriental subunit over the E487 subunit in heterotetrameric human liver mitochondrial aldehyde dehydrogenase

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Steady-state and pre-steady-state kinetics of coenzyme A linked aldehyde dehydrogenase from Escherichia coli

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Critical Glutamic Acid Residues Affecting the Mechanism and Nucleotide Specificity of Vibrio Harveyi Aldehyde Dehydrogenase

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based on heuristic

inferred from PubMed ID database lookup

Identifiers

DOI

10.1042/BJ20051525

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1666003

OpenCitations bibliographic resource ID

1666003

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1666003

PMC publication ID

1409689

0 references

PubMed publication ID

16332250

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1666003

ResearchGate publication ID

7437881

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