(Q27650766)

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Structural, functional and calorimetric investigation of MosA, a dihydrodipicolinate synthase from Sinorhizobium meliloti l5-30, does not support involvement in rhizopine biosynthesis

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Structural, functional and calorimetric investigation of MosA, a dihydrodipicolinate synthase from Sinorhizobium meliloti l5-30, does not support involvement in rhizopine biosynthesis (English)

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main subject

Sinorhizobium meliloti

object named as

Sinorhizobium meliloti

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Christopher P Phenix

1

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Kurt Nienaber

series ordinal

2

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Pui Hang Tam

series ordinal

3

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Louis T J Delbaere

series ordinal

4

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David R J Palmer

series ordinal

5

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publication date

2 July 2008

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published in

ChemBioChem

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volume

9

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issue

10

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page(s)

1591-602

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cites work

The determination of enzyme inhibitor constants

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Crossref

reference URL

https://api.crossref.org/works/10.1002%2FCBIC.200700569

retrieved

21 January 2018

Escherichia coli dihydrodipicolinate synthase. Identification of the active site and crystallization

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1002%2FCBIC.200700569

retrieved

21 January 2018

Escherichia coli dihydrodipicolinate synthase: characterization of the imine intermediate and the product of bromopyruvate treatment by electrospray mass spectrometry

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1002%2FCBIC.200700569

retrieved

21 January 2018

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DOI

10.1002/CBIC.200700569

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release_2y66t5z2qracde7xfjsoybiore

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reference URL

https://api.fatcat.wiki/v0/release/2y66t5z2qracde7xfjsoybiore

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24 November 2022

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PubMed ID

18536061

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ResearchGate publication ID

5321628

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(Q27650766)

Structural, functional and calorimetric investigation of MosA, a dihydrodipicolinate synthase from Sinorhizobium meliloti l5-30, does not support involvement in rhizopine biosynthesis

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