Related Experiment Video

Updated: Aug 6, 2026

An Assay for Measuring the Activity of Escherichia coli Inducible Lysine Decarboxyase
08:08

An Assay for Measuring the Activity of Escherichia coli Inducible Lysine Decarboxyase

Published on: December 19, 2010

An activity from Escherichia coli membranes responsible for the modification of nitrate reductase to its precursor

G R Chaudhry, I M Chaiken, C H MacGregor

    The Journal of Biological Chemistry
    |May 10, 1983
    PubMed

    More Related Videos

    Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain14:25

    Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain

    Published on: December 12, 2017

    Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET12:07

    Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET

    Published on: October 9, 2021

    Related Concept Videos

    Protein Modifications in the RER01:26

    Protein Modifications in the RER

    Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
    Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
    Export of Misfolded Proteins out of the ER01:32

    Export of Misfolded Proteins out of the ER

    After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
    Preparation of Amines: Reduction of Oximes and Nitro Compounds01:29

    Preparation of Amines: Reduction of Oximes and Nitro Compounds

    Oximes can be reduced to primary amines using catalytic hydrogenation, hydride reduction, or sodium metal reduction. The reduction of aliphatic and aromatic nitro compounds to primary amines takes place by either catalytic hydrogenation or by using active metals like Fe, Zn, and Sn in the presence of an acid.
    Though catalytic hydrogenation can reduce nitrobenzenes, the reduction is nonselective in the presence of other functional groups. For instance, if nitrobenzene contains an aldehyde group,...
    Inorganic Nitrogen Assimilation01:22

    Inorganic Nitrogen Assimilation

    Nitrogen is an essential element in biological systems, forming a crucial component of proteins, nucleic acids, and other cellular constituents. Many bacteria and archaea acquire nitrogen in the form of nitrate (NO₃⁻) or ammonia (NH₃), which are then assimilated into biomolecules through specific enzymatic pathways.Assimilatory Nitrate ReductionWhen nitrate enters the cell, it undergoes a two-step reduction process known as assimilatory nitrate reduction. Initially, the enzyme nitrate reductase...
    Bacterial Protein Maturation01:26

    Bacterial Protein Maturation

    Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
    Chemotaxis in E. coli01:27

    Chemotaxis in E. coli

    Chemotaxis in Escherichia coli is a sensory-driven motility mechanism that enables bacteria to navigate chemical gradients, moving toward beneficial environments while avoiding harmful conditions. This process relies on a signal transduction system integrating external chemical cues with flagellar motor control.Chemoreceptors and Signal DetectionE. coli detects chemical gradients through methyl-accepting chemotaxis proteins (MCPs), which are membrane-bound chemoreceptors that sense attractants...