UB Paderborn / Katalog / Suche / in CDI

1 – 25 von 112

Sortiert nach

PYRIDOXAL PHOSPHATE ENZYMES: Mechanistic, Structural, and Evolutionary Considerations

Annual review of biochemistry, 2004-01, Vol.73 (1), p.383-415

2004

Link zum Volltext

Verfügbarkeit prüfen

Biosynthesis of 2-Hydroxyethylphosphonate, an Unexpected Intermediate Common to Multiple Phosphonate Biosynthetic Pathways

The Journal of biological chemistry, 2008-08, Vol.283 (34), p.23161-23168

2008

Link zum Volltext

Verfügbarkeit prüfen

Fosmidomycin biosynthesis diverges from related phosphonate natural products

Nature chemical biology, 2019-11, Vol.15 (11), p.1049

2019

Link zum Volltext

Verfügbarkeit prüfen

Reassignment of the Structure of the Antibiotic A53868 Reveals an Unusual Amino Dehydrophosphonic Acid

Angewandte Chemie (International ed.), 2007-01, Vol.46 (47), p.9089-9092

2007

Link zum Volltext

Verfügbarkeit prüfen

The Dual-Specific Active Site of 7,8-Diaminopelargonic Acid Synthase and the Effect of the R391A Mutation

Biochemistry (Easton), 2002-10, Vol.41 (42), p.12582-12589

2002

Link zum Volltext

Verfügbarkeit prüfen

Structural basis for reduced activity of 1-aminocyclopropane-1-carboxylate synthase affected by a mutation linked to andromonoecy

FEBS letters, 2011-01, Vol.585 (1), p.111-114

2011

Link zum Volltext

Verfügbarkeit prüfen

Structure of ACC synthase inactivated by the mechanism-based inhibitor l-vinylglycine

FEBS letters, 2005-04, Vol.579 (11), p.2458-2462

2005

Link zum Volltext

Verfügbarkeit prüfen

S-Methylmethionine is both a substrate and an inactivator of 1-aminocyclopropane-1-carboxylate synthase

Archives of biochemistry and biophysics, 2004, Vol.421 (1), p.85-90

2004

Link zum Volltext

Verfügbarkeit prüfen

Avoiding the Road Less Traveled: How the Topology of Enzyme−Substrate Complexes Can Dictate Product Selection

Accounts of chemical research, 2003-10, Vol.36 (10), p.757-765

2003

Link zum Volltext

Verfügbarkeit prüfen

Conserved and Nonconserved Residues in the Substrate Binding Site of 7,8-Diaminopelargonic Acid Synthase from Escherichia coli Are Essential for Catalysis

Biochemistry (Easton), 2004-02, Vol.43 (5), p.1213-1222

2004

Link zum Volltext

Verfügbarkeit prüfen

Cofactor Requirements and Reconstitution Of Microcin B17 Synthetase: A Multienzyme Complex that Catalyzes the Formation of Oxazoles and Thiazoles in the Antibiotic Microcin B17

Biochemistry (Easton), 1999-04, Vol.38 (15), p.4768-4781

1999

Link zum Volltext

Verfügbarkeit prüfen

Cloning, Expression, and Biochemical Characterization of Streptomyces rubellomurinus Genes Required for Biosynthesis of Antimalarial Compound FR900098

Chemistry & biology, 2008-08, Vol.15 (8), p.765-770

2008

Link zum Volltext

Verfügbarkeit prüfen

ATP/GTP Hydrolysis Is Required for Oxazole and Thiazole Biosynthesis in the Peptide Antibiotic Microcin B17

Biochemistry (Easton), 1998-09, Vol.37 (38), p.13250-13261

1998

Link zum Volltext

Verfügbarkeit prüfen

Aminotransferase Activity and Bioinformatic Analysis of 1-Aminocyclopropane-1-carboxylate Synthase

Biochemistry (Easton), 2000-12, Vol.39 (49), p.15242-15249

2000

Link zum Volltext

Verfügbarkeit prüfen

Structure of 1-aminocyclopropane-1-carboxylate synthase in complex with an amino-oxy analogue of the substrate: implications for substrate binding

Biochimica et biophysica acta, 2003-04, Vol.1647 (1), p.55-60

2003

Link zum Volltext

Verfügbarkeit prüfen

Molecular Cloning and Heterologous Expression of the Dehydrophos Biosynthetic Gene Cluster

Chemistry & biology, 2010-04, Vol.17 (4), p.402-411

2010

Link zum Volltext

Verfügbarkeit prüfen

Modulation of the Internal Aldimine pKa's of 1-Aminocyclopropane-1-carboxylate Synthase and Aspartate Aminotransferase by Specific Active Site Residues

Biochemistry (Easton), 2002-03, Vol.41 (11), p.3836-3842

2002

Link zum Volltext

Verfügbarkeit prüfen

Biosynthesis of 2-Hydroxyethylphosphonate, an Unexpected Intermediate Common to Multiple Phosphonate Biosynthetic PathwaysS

The Journal of biological chemistry, 2008-08, Vol.283 (34), p.23161-23168

2008

Link zum Volltext

Verfügbarkeit prüfen

Modulation of the internal aldimine pK(a)'s of 1-aminocyclopropane-1-carboxylate synthase and aspartate aminotransferase by specific active site residues

Biochemistry (Easton), 2002-03, Vol.41 (11), p.3836

2002

Link zum Volltext

Verfügbarkeit prüfen

Modulation of the Internal Aldimine p K a 's of 1-Aminocyclopropane-1-carboxylate Synthase and Aspartate Aminotransferase by Specific Active Site Residues

Biochemistry (Easton), 2002-03, Vol.41 (11), p.3836-3842

2002

Link zum Volltext

Verfügbarkeit prüfen

Reassignment of the Structure of the Antibiotic A53868 Reveals an Unusual Amino Dehydrophosphonic Acid

Angewandte Chemie, 2007-12, Vol.119 (47), p.9247-9250

2007

Link zum Volltext

Verfügbarkeit prüfen

Reassignment of the Structure of the Antibiotic A53868 Reveals an Unusual Amino Dehydrophosphonic Acid

Angewandte Chemie, 2007-12, Vol.119 (47), p.9247-9250

2007

Link zum Volltext

Verfügbarkeit prüfen

Modulation of the Internal Aldimine pK a's of 1-Aminocyclopropane-1-carboxylate Synthase and Aspartate Aminotransferase by Specific Active Site Residues

Biochemistry (Easton), 2002-03, Vol.41 (11), p.3836-3842

2002

Link zum Volltext

Verfügbarkeit prüfen

Avoiding the Road Less Traveled: How the Topology of Enzyme-Substrate Complexes Can Dictate Product Selection

ChemInform, 2004-01, Vol.35 (3), p.no-no

2004

Link zum Volltext

Verfügbarkeit prüfen

Biosynthesis of the Potent Antimalarial Compound FR900098

Chemistry & biology, 2008-08, Vol.15 (8), p.765-770

2008

Link zum Volltext

Verfügbarkeit prüfen

1 – 25 von 112

Suche als RSS-Feed

Suchergebnisse filtern

Filter anzeigen

Nur zeigen

Geprüft (Peer-Review)
(98)
Mit Volltextzugriff
(107)

Publikationsform

Sprache

Englisch
(110)
Japanisch
(25)
Deutsch
(1)

Erscheinungsjahr

n.n

Thema

15 weitere anzeigen...

Weniger anzeigen...

Menü

Weitere Dienste

Einstellungen

PYRIDOXAL PHOSPHATE ENZYMES: Mechanistic, Structural, and Evolutionary Considerations

Biosynthesis of 2-Hydroxyethylphosphonate, an Unexpected Intermediate Common to Multiple Phosphonate Biosynthetic Pathways

Fosmidomycin biosynthesis diverges from related phosphonate natural products

Reassignment of the Structure of the Antibiotic A53868 Reveals an Unusual Amino Dehydrophosphonic Acid

The Dual-Specific Active Site of 7,8-Diaminopelargonic Acid Synthase and the Effect of the R391A Mutation

Structural basis for reduced activity of 1-aminocyclopropane-1-carboxylate synthase affected by a mutation linked to andromonoecy

Structure of ACC synthase inactivated by the mechanism-based inhibitor l-vinylglycine

S-Methylmethionine is both a substrate and an inactivator of 1-aminocyclopropane-1-carboxylate synthase

Avoiding the Road Less Traveled: How the Topology of Enzyme−Substrate Complexes Can Dictate Product Selection

Conserved and Nonconserved Residues in the Substrate Binding Site of 7,8-Diaminopelargonic Acid Synthase from Escherichia coli Are Essential for Catalysis

Cofactor Requirements and Reconstitution Of Microcin B17 Synthetase: A Multienzyme Complex that Catalyzes the Formation of Oxazoles and Thiazoles in the Antibiotic Microcin B17

Cloning, Expression, and Biochemical Characterization of Streptomyces rubellomurinus Genes Required for Biosynthesis of Antimalarial Compound FR900098

ATP/GTP Hydrolysis Is Required for Oxazole and Thiazole Biosynthesis in the Peptide Antibiotic Microcin B17

Aminotransferase Activity and Bioinformatic Analysis of 1-Aminocyclopropane-1-carboxylate Synthase

Structure of 1-aminocyclopropane-1-carboxylate synthase in complex with an amino-oxy analogue of the substrate: implications for substrate binding

Molecular Cloning and Heterologous Expression of the Dehydrophos Biosynthetic Gene Cluster

Modulation of the Internal Aldimine pKa's of 1-Aminocyclopropane-1-carboxylate Synthase and Aspartate Aminotransferase by Specific Active Site Residues

Biosynthesis of 2-Hydroxyethylphosphonate, an Unexpected Intermediate Common to Multiple Phosphonate Biosynthetic PathwaysS

Modulation of the internal aldimine pK(a)'s of 1-aminocyclopropane-1-carboxylate synthase and aspartate aminotransferase by specific active site residues

Modulation of the Internal Aldimine p K a 's of 1-Aminocyclopropane-1-carboxylate Synthase and Aspartate Aminotransferase by Specific Active Site Residues

Reassignment of the Structure of the Antibiotic A53868 Reveals an Unusual Amino Dehydrophosphonic Acid

Reassignment of the Structure of the Antibiotic A53868 Reveals an Unusual Amino Dehydrophosphonic Acid

Modulation of the Internal Aldimine pK a's of 1-Aminocyclopropane-1-carboxylate Synthase and Aspartate Aminotransferase by Specific Active Site Residues

Avoiding the Road Less Traveled: How the Topology of Enzyme-Substrate Complexes Can Dictate Product Selection

Biosynthesis of the Potent Antimalarial Compound FR900098

Suchergebnisse filtern