One of the most important glycolytic genes is fructose-1,6-bisphosphate aldolase (fbaA).

This cleavage is very similar mechanistically to the aldolase A reaction of glycolysis.

The aldolase used in gluconeogenesis and glycolysis is a cytoplasmic protein.

This gene encodes a member of the class I fructose-bisphosphate aldolase gene family.

Each subunit contains a phosphate-ion bound in position of the aldolase biding site.

Fructose-1-phosphate is metabolized by aldolase B into dihydroxyacetone phosphate and glyceraldehyde.

In bacterial systems, sialic acids are biosynthesized by an aldolase enzyme.

Some defects in aldolase B cause hereditary fructose intolerance.

If fructose is ingested, the enzymatic block at aldolase B causes an accumulation of fructose-1-phosphate.

Identification of a cysteinyl residue involved in the activity of rabbit muscle aldolase.

On the mechanism of formation of a partially active aldolase by tryptic digestion.

The active site of this archaeal aldolase is also in a TIM barrel.

HFI is caused by a deficiency of aldolase B.

PfRH2b also binds aldolase with its cytoplasmic tail.

Another part of the explanation was the presumed complexity of aldolase catalysis that dominated chemical thinking for a long time.

The evolved aldolase is capable of accepting both D- and L-glyceraldehyde in their non-phosphorylated form.

This is the same mechanism proposed by Barbas for aldolase antibodies reported by the group in 1995:

The word often refers to any type of fructose-bisphosphate aldolase, but can also refer to other enzymes, such as the one that forms sialic acid.

A remarkable feature of the structure is that it shows a very close resemblance to that of L-fuculose-phosphate aldolase.

The resultant glyceraldehyde formed by aldolase B then undergoes phosphorylation to glyceraldehyde 3-phosphate.

PfLRH2a does not bind aldolase.

Genetic mutations leading to defects in aldolase B result in a condition called hereditary fructose intolerance.

The aldolase used by plants and algae in the Calvin cycle is usually a plastid-targeted protein encoded by a nuclear gene.

The second enzyme of the L-carnitine biosynthetic pathway pathway is 3-hydroxy-N-trimethyllysine aldolase.

In bacteria, acylating acetaldehyde dehydrogenase forms a bifunctional heterodimer with metal-dependent 4-hydroxy-2-ketovalerate aldolase.