The versatility of phosphoenolpyruvate and its vinyl ether products in biosynthesis (Q41112852)

26 September 2017

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title

The versatility of phosphoenolpyruvate and its vinyl ether products in biosynthesis (English)

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26 September 2017

Walsh CT

1

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26 September 2017

Benson TE

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2

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26 September 2017

Kim DH

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3

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26 September 2017

Lees WJ

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4

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26 September 2017

1 February 1996

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26 September 2017

Chemistry and Biology

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26 September 2017

3

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26 September 2017

2

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26 September 2017

83-91

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Phosphonate biosynthesis: isolation of the enzyme responsible for the formation of a carbon-phosphorus bond.

26 September 2017

1 reference

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Mechanism of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthetase.

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3-Deoxy-D-manno-octulosonate-8-phosphate synthase catalyzes the C-O bond cleavage of phosphoenolpyruvate

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Overproduction and one-step purification of Escherichia coli 3-deoxy-D-manno-octulosonic acid 8-phosphate synthase and oxygen transfer studies during catalysis using isotopic-shifted heteronuclear NMR.

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Stereochemistry of 3-deoxyoctulosonate 8-phosphate synthase

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Catalytic mechanism of 3-deoxy-D-manno-2-octulosonate-8-phosphate synthase. The use of synthetic analogues to probe the structure of the putative reaction intermediate

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The herbicide glyphosate is a potent inhibitor of 5-enolpyruvyl-shikimic acid-3-phosphate synthase

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The mechanism of action of fosfomycin (phosphonomycin)

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A tetrahedral intermediate in the EPSP synthase reaction observed by rapid quench kinetics

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Detection and characterization of a phospholactoyl-enzyme adduct in the reaction catalyzed by UDP-N-acetylglucosamine enolpyruvoyl transferase, MurZ

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Overexpression, purification, and characterization of isochorismate synthase (EntC), the first enzyme involved in the biosynthesis of enterobactin from chorismate

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New insight into the catalytic mechanism of chorismate mutases from structural studies

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Subcloning of the enterobactin biosynthetic gene entB: expression, purification, characterization, and substrate specificity of isochorismatase.

1 reference

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Mechanistic studies on trans-2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (Ent A) in the biosynthesis of the iron chelator enterobactin

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Overexpression, purification, and mechanistic study of UDP-N-acetylenolpyruvylglucosamine reductase

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An enzyme-substrate complex involved in bacterial cell wall biosynthesis

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(E)-enolbutyryl-UDP-N-acetylglucosamine as a mechanistic probe of UDP-N-acetylenolpyruvylglucosamine reductase (MurB)

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7 January 2021

10.1016/S1074-5521(96)90282-3

Identifiers

DOI

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26 September 2017

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