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Alternatively the C-terminal catalytic region is highly conserved and constitutes the mature enzyme. The first three-dimensional structure solved for a plant pectinesterase was for an isoform from carrot (Daucus carota) root and consists of a right-handed parallel β-helix as seen in all the carbohydrate esterase family CE-8, a transmembrane ...
The zymogenic form of plant APs contain the primary sequence of the PSI, although not all plant APs contain a PSI region. [4] The PSI itself is composed of approximately 100 residues and is found in the C-terminal primary structure of zymogenic plant APs, forming an independent domain from the characteristic bilobal tertiary structure of aspartic proteases.
This structure accounts for its astonishing 'refractory' nature toward various 'denaturing' agents: all germins share a remarkable stability when subjected to heat, detergents, extreme pH and resistance to broad specificity proteolytic (digestive) enzymes. Seed storage proteins of grasses and cereals belong to the eponymous prolamin superfamily ...
Enzymes are generally globular proteins, acting alone or in larger complexes. The sequence of the amino acids specifies the structure which in turn determines the catalytic activity of the enzyme. [25] Although structure determines function, a novel enzymatic activity cannot yet be predicted from structure alone. [26]
EPSP synthase is a monomeric enzyme with a molecular mass of approximately 46,000. [2] [3] [4] It consists of two domains connected by protein strands that function as a hinge, allowing the two domains to move closer together.
The acetolactate synthase (ALS) enzyme (also known as acetohydroxy acid or acetohydroxyacid synthase, abbr. AHAS) [2] is a protein found in plants and micro-organisms. ALS catalyzes the first step in the synthesis of the branched-chain amino acids (valine, leucine, and isoleucine).
The Fe protein, the dinitrogenase reductase or NifH, is a dimer of identical subunits which contains one [Fe 4 S 4] cluster and has a mass of approximately 60-64kDa. [2] The function of the Fe protein is to transfer electrons from a reducing agent, such as ferredoxin or flavodoxin to the nitrogenase protein.
Phytate. A phytase (myo-inositol hexakisphosphate phosphohydrolase) is any type of phosphatase enzyme that catalyzes the hydrolysis of phytic acid (myo-inositol hexakisphosphate) – an indigestible, organic form of phosphorus that is found in many plant tissues, especially in grains and oil seeds – and releases a usable form of inorganic phosphorus. [1]