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The active site of this enzyme is in the center of the barrel. A glutamic acid residue and a histidine are involved in the catalytic mechanism. The sequence around the active site residues is conserved in all known triose phosphate isomerases. The structure of triose phosphate isomerase contributes to its function.
TIGAR is a single enzyme with dual function that regulates F2,6BP. It can behave as a phosphatase (fructuose-2,6-bisphosphatase) which cleaves the phosphate at carbon-2 producing F6P. It can also behave as a kinase (PFK2) adding a phosphate onto carbon-2 of F6P which produces F2,6BP. In humans, the TIGAR protein is encoded by C12orf5 gene. The ...
This form is composed of four identical 37-kDa subunits containing a single catalytic thiol group each and critical to the enzyme's catalytic function. [6] [7] Nuclear GAPDH has increased isoelectric point (pI) of pH 8.3–8.7. [7] Of note, the cysteine residue C152 in the enzyme's active site is required for the induction of apoptosis by ...
The protein encoded by this gene is a dimeric enzyme that catalyzes the reversible isomerization of G6P and F6P. [12] [13] Since the reaction is reversible, its direction is determined by G6P and F6P concentrations. [9] glucose 6-phosphate ↔ fructose 6-phosphate. The protein has different functions inside and outside the cell.
Pyruvate decarboxylase occurs as a dimer of dimers with two active sites shared between the monomers of each dimer. The enzyme contains a beta-alpha-beta structure, yielding parallel beta-sheets. It contains 563 residue subunits in each dimer; the enzyme has strong intermonomer attractions, but the dimers loosely interact to form a loose ...
In humans, two isozymes of PGK have been so far identified, PGK1 and PGK2. The isozymes have 87-88% identical amino acid sequence identity and though they are structurally and functionally similar, they have different localizations: PGK2, encoded by an autosomal gene, is unique to meiotic and postmeiotic spermatogenic cells, while PGK1, encoded ...
Linoleoyl-CoA desaturase (also Delta 6 desaturase, EC 1.14.19.3) is an enzyme that converts between types of fatty acids, which are essential nutrients in the human body. The enzyme mainly catalyzes the chemical reaction. linoleoyl-CoA + AH 2 + O 2 gamma-linolenoyl-CoA + A + 2 H 2 O
Cyanobacterial DesA, [19] an enzyme that can introduce a second cis double bond at the delta-12 position of fatty acid bound to membrane glycerolipids. This enzyme is involved in chilling tolerance; the phase transition temperature of lipids of cellular membranes being dependent on the degree of unsaturation of fatty acids of the membrane lipids.