L-fuculose-phosphate aldolase | |||||||||
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Identifiers | |||||||||
EC no. | 4.1.2.17 | ||||||||
CAS no. | 9024-54-8 | ||||||||
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 L-fuculose-phosphate aldolase (EC 4.1.2.17) 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-fuculose-1-phosphate (S)-lactaldehyde-lyase (glycerone-phosphate-forming). Other names in common use include L-fuculose 1-phosphate aldolase, fuculose aldolase, and L-fuculose-1-phosphate lactaldehyde-lyase. This enzyme participates in fructose and mannose metabolism.
As of late 2007, 20 structures have been solved for this class of enzymes, with PDB accession codes 1DZU, 1DZV, 1DZW, 1DZX, 1DZY, 1DZZ, 1E46, 1E47, 1E48, 1E49, 1E4A, 1E4B, 1E4C, 1FUA, 2FK5, 2FLF, 2FUA, 2OPI, 3FUA, and 4FUA.
In enzymology, a L-fucose isomerase 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.
The enzyme 2-dehydro-3-deoxy-phosphogluconate aldolase, commonly known as KDPG aldolase, catalyzes the chemical reaction
The enzyme 3-deoxy-D-manno-octulosonate aldolase 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 indole-3-glycerol-phosphate synthase (IGPS) (EC 4.1.1.48) catalyzes the chemical reaction
The enzyme ketotetrose-phosphate aldolase catalyzes the chemical reaction
The enzyme phosphatidylserine decarboxylase (EC 4.1.1.65) catalyzes the chemical reaction
The enzyme rhamnulose-1-phosphate aldolase (EC 4.1.2.19) 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
In enzymology, a threonine-tRNA ligase is an enzyme that catalyzes the chemical reaction
The enzyme chondroitin B lyase catalyzes the following process:
The enzyme imidazoleglycerol-phosphate dehydratase (EC 4.2.1.19) catalyzes the chemical reaction
In enzymology, a DNA beta-glucosyltransferase is an enzyme that catalyzes the chemical reaction in which a beta-D-glucosyl residue is transferred from UDP-glucose to an hydroxymethylcytosine residue in DNA. It is analogous to the enzyme DNA alpha-glucosyltransferase.
In enzymology, a nucleoside-phosphate kinase is an enzyme that catalyzes the chemical reaction
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.