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Blatant Biology
Biochemistry 2, L1 definitions
Bulk protein degradation
the mass hydrolysis of proteins; a pathway that can (and is) tightly controlled to prevent excessive protein degradation
Catalytic dyad
a pair of amino acids catalysing a reaction in an enzyme; can be conserved across enzymes catalysing the same reaction
Thioacyl enzyme intermediate
the product left bound in the active site of a cysteine protease, after product 1 has left but before hydrolysis of a water molecule occurs to reset the enzyme to its original form
Deamidation enzyme
enzyme catalysing the removal of an amide functional group (on aspargine, aspartic acids, isoaspartic acid residues); alters the structure, function, and stability of a protein (potentially accelerating degradation)
Burkholderia
genus of pathogenic bacteria, causing many challenging infections that are multi-drug resistant infections; infection may present with the signs and symptoms of other common illnesses (such as TB)
Cognate protein
an identical protein found in a different species
BPSL1549
a toxin protein from burkholderia pseudomallei, with a similar function to CNF1 from E. coli
CNF1
a protein toxin produced by some pathogenic strains of E. coli
Glutamine deaminase
enzyme catalysing the deamination of glutamine amino acids
Spatial conservation
the maintenance of the 3D arrangment of catalytic residues in an enzyme, allowing the same reaction to be catalysed; frequently seen across enzymes with the same catalytic function
Papain
family of proteases isolated from papya, with wide ranging uses; has a catalytic triad
Rho
small GTPase protein, regulating actin dynamics in many cells; act as molecular switches, controlling organelle development, cytoskeletal dynamics, cell movement, ...; deamidated by CNF1
Rac
protein found in human cells, controlling GLUT4 translocation, cell growth, cytoskeletal reorganisation, ...; deamidated by CNF1
cdc42
protein regulating the cell cycle, mediating cell division; deamidated by CNF1
Necrotising
inducing uncontrolled cell death by apoptosis in the host organism
Enolase superfamily
large family of enzymes catalysing a wide range of metabolic reactions; all reactions involve the abstraction of a proton from a carbon adjacent to a carboxylic acid, and all have a divalent metal ion
Divalent Metal Ion
metal ions that are positively charged and have a 2+ positive charge
Mandelate racemase
bacterial enzyme catalysing the interconversin of enantiomers of mandelate through an enol intermediate
Chirality
a molecule with a non-superimposable mirror image
Metal ion catalysis
a type of acid-base catalysis supported by a metal ion
Acid-base catalysis
a catalytic reaction supported by an acid or base
Capping domain
the protein domain within the enolase superfamily that contains the specificity pocket
Muconate lactonising enzyme, MLE
member of the enolase superfamily, containing 2 proteins and 2 magnesium ions; catalyses the protonation of the enolate alpha-carbon (opposite reaction of beta-elimination)
Beta Elimination
the removal of the beta carbon, allowing the formation of a bond between the alpha and gamma carbons; catalysed by muconate lactonising enzyme
Mandelate racemase, MR
enzyme catalysing the interconversion between mandalate enantiomers, through an enol intermediate
Capping barrel domain
a beta-barrel containing the active site residues of an enzyme, such as within muconate lactonising enzyme