rhamnulose-1-phosphate aldolase | |||||||||
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Identifiers | |||||||||
EC no. | 4.1.2.19 | ||||||||
CAS no. | 9054-58-4 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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The enzyme rhamnulose-1-phosphate aldolase (EC 4.1.2.19) catalyzes the chemical reaction
This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is L-rhamnulose-1-phosphate (S)-lactaldehyde-lyase (glycerone-phosphate-forming). Other names in common use include rhamnulose phosphate aldolase, L-rhamnulose 1-phosphate aldolase, L-rhamnulose-phosphate aldolase, and L-rhamnulose-1-phosphate lactaldehyde-lyase. This enzyme participates in pentose and glucuronate interconversions and fructose and mannose metabolism.
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1GT7 and 1OJR.
Fructose-bisphosphate aldolase, often just aldolase, is an enzyme catalyzing a reversible reaction that splits the aldol, fructose 1,6-bisphosphate, into the triose phosphates dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (G3P). Aldolase can also produce DHAP from other (3S,4R)-ketose 1-phosphates such as fructose 1-phosphate and sedoheptulose 1,7-bisphosphate. Gluconeogenesis and the Calvin cycle, which are anabolic pathways, use the reverse reaction. Glycolysis, a catabolic pathway, uses the forward reaction. Aldolase is divided into two classes by mechanism.
In enzymology, a glycerol-3-phosphate dehydrogenase [NAD(P)+] (EC 1.1.1.94) is an enzyme that catalyzes the chemical reaction
In enzymology, a L-ribulose-5-phosphate 4-epimerase is an enzyme that catalyzes the interconversion of ribulose 5-phosphate and xylulose 5-phosphate in the oxidative phase of the Pentose phosphate pathway.
Cystathionine beta-lyase, also commonly referred to as CBL or β-cystathionase, is an enzyme that primarily catalyzes the following α,β-elimination reaction
The enzyme 2-dehydro-3-deoxy-phosphogluconate aldolase, commonly known as KDPG aldolase, catalyzes the chemical reaction
The enzyme 3-dehydro-L-gulonate-6-phosphate decarboxylase (EC 4.1.1.85) catalyzes the chemical reaction
The enzyme 4-hydroxy-2-oxoglutarate aldolase catalyzes the chemical reaction
The enzyme 5-dehydro-2-deoxyphosphogluconate aldolase catalyzes the chemical reaction
The enzyme ketotetrose-phosphate aldolase catalyzes the chemical reaction
The enzyme L-fuculose-phosphate aldolase (EC 4.1.2.17) catalyzes the chemical reaction
The enzyme phosphatidylserine decarboxylase (EC 4.1.1.65) catalyzes the chemical reaction
The enzyme tagatose-bisphosphate aldolase catalyzes the chemical reaction
The enzyme threonine aldolase is an enzyme that catalyzes the chemical reaction
The enzyme tryptophanase (EC 4.1.99.1) catalyzes the chemical reaction
The enzyme imidazoleglycerol-phosphate dehydratase (EC 4.2.1.19) catalyzes the chemical reaction
The enzyme methylglyoxal synthase catalyzes the chemical reaction
In enzymology, a cystathionine gamma-synthase is an enzyme that catalyzes the formation of cystathionine from cysteine and an activated derivative of homoserine, e.g.:
In enzymology, a rhamnulokinase is an enzyme that catalyzes the chemical reaction
3-Deoxy-D-arabinoheptulosonate 7-phosphate (DAHP) synthase is the first enzyme in a series of metabolic reactions known as the shikimate pathway, which is responsible for the biosynthesis of the amino acids phenylalanine, tyrosine, and tryptophan. Since it is the first enzyme in the shikimate pathway, it controls the amount of carbon entering the pathway. Enzyme inhibition is the primary method of regulating the amount of carbon entering the pathway. Forms of this enzyme differ between organisms, but can be considered DAHP synthase based upon the reaction that is catalyzed by this enzyme.
Low-specificity L-threonine aldolase is an enzyme with systematic name L-threonine/L-allo-threonine acetaldehyde-lyase (glycine-forming). This enzyme catalyses the following chemical reaction