(Q30320522)

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A proposed mechanism for the reductive ring opening of the cyclodiphosphate MEcPP, a crucial transformation in the new DXP/MEP pathway to isoprenoids based on modeling studies and feeding experiments

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scholarly article

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Europe PubMed Central

PubMed publication ID

17 June 2017

A proposed mechanism for the reductive ring opening of the cyclodiphosphate MEcPP, a crucial transformation in the new DXP/MEP pathway to isoprenoids based on modeling studies and feeding experiments (English)

1 reference

Europe PubMed Central

PubMed publication ID

17 June 2017

Ludger A Wessjohann

6

object named as

Ludger A Wessjohann

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Europe PubMed Central

PubMed publication ID

17 June 2017

author name string

Wolfgang Brandt

1

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Europe PubMed Central

PubMed publication ID

17 June 2017

Marco A Dessoy

2

1 reference

Europe PubMed Central

PubMed publication ID

17 June 2017

Michael Fulhorst

3

1 reference

Europe PubMed Central

PubMed publication ID

17 June 2017

Wenyun Gao

4

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17 June 2017

Meinhart H Zenk

5

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Europe PubMed Central

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17 June 2017

publication date

1 March 2004

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Europe PubMed Central

PubMed publication ID

17 June 2017

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Europe PubMed Central

PubMed publication ID

17 June 2017

5

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Europe PubMed Central

PubMed publication ID

17 June 2017

3

1 reference

Europe PubMed Central

PubMed publication ID

17 June 2017

311-323

1 reference

Europe PubMed Central

PubMed publication ID

17 June 2017

Cytidine 5'-triphosphate-dependent biosynthesis of isoprenoids: YgbP protein of Escherichia coli catalyzes the formation of 4-diphosphocytidyl-2-C-methylerythritol

1 reference

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Biosynthesis of terpenoids: YchB protein of Escherichia coli phosphorylates the 2-hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol

1 reference

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Biosynthesis of terpenoids: YgbB protein converts 4-diphosphocytidyl-2C-methyl-D-erythritol 2-phosphate to 2C-methyl-D-erythritol 2,4-cyclodiphosphate

1 reference

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1 reference

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Crystal structure of 1-deoxy-D-xylulose-5-phosphate reductoisomerase, a crucial enzyme in the non-mevalonate pathway of isoprenoid biosynthesis

1 reference

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Structure of 2C-methyl-D-erythritol 2,4- cyclodiphosphate synthase: an essential enzyme for isoprenoid biosynthesis and target for antimicrobial drug development

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1-Deoxy-D-xylulose-5-phosphate synthase, a limiting enzyme for plastidic isoprenoid biosynthesis in plants

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Biosynthesis of terpenoids: 1-deoxy-D-xylulose-5-phosphate reductoisomerase from Escherichia coli is a class B dehydrogenase

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Studies on the nonmevalonate pathway to terpenes: the role of the GcpE (IspG) protein

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Isoprenoid biosynthesis through the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase (GcpE) is a [4Fe-4S] protein

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Identification of (E)-4-hydroxy-3-methyl-but-2-enyl pyrophosphate as a major activator for human gammadelta T cells in Escherichia coli

1 reference

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LytB protein catalyzes the terminal step of the 2-C-methyl-D-erythritol-4-phosphate pathway of isoprenoid biosynthesis

1 reference

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Functional characterization of GcpE, an essential enzyme of the non-mevalonate pathway of isoprenoid biosynthesis

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Studies on the nonmevalonate pathway of terpene biosynthesis. The role of 2C-methyl-D-erythritol 2,4-cyclodiphosphate in plants

1 reference

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(E)-4-Hydroxy-3-methylbut-2-enyl diphosphate: an intermediate in the formation of terpenoids in plant chromoplasts

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Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)

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Mild oxidation of alcohols with o-iodoxybenzoic acid (IBX) in water/acetone mixture in the presence of beta-cyclodextrin

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Isoprenoid biosynthesis via the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate reductase (LytB/IspH) from Escherichia coli is a [4Fe-4S] protein.

1 reference

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The deoxyxylulose phosphate pathway of isoprenoid biosynthesis: studies on the mechanisms of the reactions catalyzed by IspG and IspH protein

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Enhanced genome annotation using structural profiles in the program 3D-PSSM

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Three-dimensional structure of M. tuberculosis dihydrofolate reductase reveals opportunities for the design of novel tuberculosis drugs

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FeMo cofactor of nitrogenase: a density functional study of states M(N), M(OX), M(R), and M(I).

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Prediction of protein secondary structure at better than 70% accuracy

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Readily accessible 12-I-5 oxidant for the conversion of primary and secondary alcohols to aldehydes and ketones

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Identifiers

10.1002/CBIC.200300743

1 reference

Europe PubMed Central

PubMed publication ID

17 June 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

17 June 2017

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