Page last updated: 2024-09-04

carbapenems and glutamate-1-semialdehyde

carbapenems has been researched along with glutamate-1-semialdehyde in 2 studies

Compound Research Comparison

Studies (carbapenems)	Trials (carbapenems)	Recent Studies (post-2010) (carbapenems)	Studies (glutamate-1-semialdehyde)	Trials (glutamate-1-semialdehyde)	Recent Studies (post-2010) (glutamate-1-semialdehyde)
7,355	147	5,277	14	0	3

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	2 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Schofield, CJ; Sleeman, MC	1
Batchelar, ET; McDonough, MA; Schofield, CJ; Sleeman, MC; Sorensen, JL	1

Other Studies

2 other study(ies) available for carbapenems and glutamate-1-semialdehyde

Article	Year
Carboxymethylproline synthase (CarB), an unusual carbon-carbon bond-forming enzyme of the crotonase superfamily involved in carbapenem biosynthesis. The Journal of biological chemistry, 2004, Feb-20, Volume: 279, Issue:8 Topics: Acetyl Coenzyme A; Amino Acid Sequence; Carbapenems; Carbon; Carbon-Carbon Lyases; Chromatography, Gel; Circular Dichroism; Cloning, Molecular; Dithionitrobenzoic Acid; Electrophoresis, Polyacrylamide Gel; Enoyl-CoA Hydratase; Glutamates; Glutamic Acid; Kinetics; Lactams; Magnetic Resonance Spectroscopy; Malonyl Coenzyme A; Mass Spectrometry; Models, Chemical; Molecular Sequence Data; Pectobacterium; Protein Binding; Recombinant Proteins; Sequence Homology, Amino Acid; Stereoisomerism; Thienamycins	2004
Structural and mechanistic studies on carboxymethylproline synthase (CarB), a unique member of the crotonase superfamily catalyzing the first step in carbapenem biosynthesis. The Journal of biological chemistry, 2005, Oct-14, Volume: 280, Issue:41 Topics: Aldehydes; Anhydrides; Binding Sites; Carbapenems; Carbon-Carbon Lyases; Catalysis; Chromatography, Liquid; Crystallography, X-Ray; Enoyl-CoA Hydratase; Escherichia coli; Esters; Glutamates; Glutamic Acid; Histidine; Hydrogen Bonding; Mass Spectrometry; Models, Chemical; Models, Molecular; Mutagenesis; Proline; Protein Binding; Protein Conformation; Protein Structure, Secondary; Selenomethionine; Substrate Specificity; Thiolester Hydrolases; Trypsin	2005

Article

Year

Carboxymethylproline synthase (CarB), an unusual carbon-carbon bond-forming enzyme of the crotonase superfamily involved in carbapenem biosynthesis.

The Journal of biological chemistry, 2004, Feb-20, Volume: 279, Issue:8

Topics: Acetyl Coenzyme A; Amino Acid Sequence; Carbapenems; Carbon; Carbon-Carbon Lyases; Chromatography, Gel; Circular Dichroism; Cloning, Molecular; Dithionitrobenzoic Acid; Electrophoresis, Polyacrylamide Gel; Enoyl-CoA Hydratase; Glutamates; Glutamic Acid; Kinetics; Lactams; Magnetic Resonance Spectroscopy; Malonyl Coenzyme A; Mass Spectrometry; Models, Chemical; Molecular Sequence Data; Pectobacterium; Protein Binding; Recombinant Proteins; Sequence Homology, Amino Acid; Stereoisomerism; Thienamycins

2004

Structural and mechanistic studies on carboxymethylproline synthase (CarB), a unique member of the crotonase superfamily catalyzing the first step in carbapenem biosynthesis.

The Journal of biological chemistry, 2005, Oct-14, Volume: 280, Issue:41

Topics: Aldehydes; Anhydrides; Binding Sites; Carbapenems; Carbon-Carbon Lyases; Catalysis; Chromatography, Liquid; Crystallography, X-Ray; Enoyl-CoA Hydratase; Escherichia coli; Esters; Glutamates; Glutamic Acid; Histidine; Hydrogen Bonding; Mass Spectrometry; Models, Chemical; Models, Molecular; Mutagenesis; Proline; Protein Binding; Protein Conformation; Protein Structure, Secondary; Selenomethionine; Substrate Specificity; Thiolester Hydrolases; Trypsin

2005