phosphosulfolactate synthase | |||||||||
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Identifiers | |||||||||
EC no. | 4.4.1.19 | ||||||||
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 phosphosulfolactate synthase (EC 4.4.1.19) catalyzes the reaction
This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is (2R)-2-O-phospho-3-sulfolactate hydrogen-sulfite-lyase (phosphoenolpyruvate-forming). Other names in common use include (2R)-phospho-3-sulfolactate synthase, and (2R)-O-phospho-3-sulfolactate sulfo-lyase.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1U83.
In biochemistry, a lyase is an enzyme that catalyzes the breaking of various chemical bonds by means other than hydrolysis and oxidation, often forming a new double bond or a new ring structure. The reverse reaction is also possible. For example, an enzyme that catalyzed this reaction would be a lyase:
2-C-Methyl-D-erythritol 2,4-cyclodiphosphate synthase is a zinc-dependent enzyme and a member of the YgbB N terminal protein domain, which participates in the MEP pathway of isoprenoid precursor biosynthesis. It catalyzes the following reaction:
The enzyme (2R)-sulfolactate sulfo-lyase catalyzes the reaction
The enzyme indole-3-glycerol-phosphate lyase catalyzes the chemical reaction
The enzyme methylisocitrate lyase catalyzes the chemical reaction
The enzyme 3-dehydroquinate synthase catalyzes the chemical reaction
The enzyme 6-pyruvoyltetrahydropterin synthase catalyzes the following chemical reaction:
The enzyme ethanolamine-phosphate phospho-lyase (EC 4.2.3.2) catalyzes the chemical reaction
The enzyme threonine synthase (EC 4.2.3.1) catalyzes the chemical reaction
The enzyme 2-phosphosulfolactate phosphatase (EC 3.1.3.71) catalyzes the reaction
In enzymology, a 2-methylcitrate synthase (EC 2.3.3.5) is an enzyme that catalyzes the chemical reaction
In enzymology, a 3-deoxy-8-phosphooctulonate synthase (EC 2.5.1.55) is an enzyme that catalyzes the chemical reaction
In enzymology, a N-acetylneuraminate synthase (EC 2.5.1.56) is an enzyme that catalyzes the chemical reaction
In enzymology, a N-acylneuraminate-9-phosphate synthase (EC 2.5.1.57) is an enzyme that catalyzes the chemical reaction
In enzymology, a phosphoenolpyruvate-protein phosphotransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a tau-protein kinase 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.
5-enolpyruvylshikimate-3-phosphate (EPSP) synthase is an enzyme produced by plants and microorganisms. EPSPS catalyzes the chemical reaction:
Cysteate synthase is an enzyme with systematic name sulfite:O-phospho-L-serine sulfotransferase . This enzyme catalyses the following chemical reaction