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Literature summary for 2.3.1.50 extracted from

  • Han, G.; Gable, K.; Yan, L.; Allen, M.J.; Wilson, W.H.; Moitra, P.; Harmon, J.M.; Dunn, T.M.
    Expression of a novel marine viral single-chain serine palmitoyltransferase and construction of yeast and mammalian single-chain chimera (2006), J. Biol. Chem., 281, 39935-39942.
    View publication on PubMed
Search for more literature for 2.3.1.50

Cloned(Commentary)

Cloned (Comment) Organism
gene ehv050, DNA and amino acid sequence determination and analysis, functional expression of HA-tagged enzyme in Saccharmoyces cerevisiae endoplasmic reticulum, when the two subunits of the yeast SPT are thus expressed, the single-chain chimera is functional and displays a different substrate preference, independently expressed domains of the viral SPT reassemble into an active protein, overview Coccolithovirus

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
 Coccolithovirus 5783
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Coccolithovirus the viral single-chain enzyme might form multiprotein complexes in vivo with functions different from the monomer ?
-
 ?
myristoyl-CoA + L-serine Coccolithovirus SPT is the first and rate-limiting enzyme of sphingolipid biosynthesis CoA + 2-amino-1-hydroxyhexadecan-3-one + CO2
-
 ?
palmitoyl-CoA + L-serine Coccolithovirus SPT is the first and rate-limiting enzyme of sphingolipid biosynthesis CoA + 3-dehydro-D-sphinganine + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Coccolithovirus
-
 infects the globally important marine calcifying microalga Emiliania huxleyi, gene ehv050
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the viral single-chain enzyme might form multiprotein complexes in vivo with functions different from the monomer Coccolithovirus ?
-
 ?
additional information acyl-CoA substrate specificity, overview Coccolithovirus ?
-
 ?
myristoyl-CoA + L-serine SPT is the first and rate-limiting enzyme of sphingolipid biosynthesis Coccolithovirus CoA + 2-amino-1-hydroxyhexadecan-3-one + CO2
-
 ?
myristoyl-CoA + L-serine the viral enzyme exhibits preference for myristoyl-CoA rather than palmitoyl-CoA Coccolithovirus CoA + 2-amino-1-hydroxyhexadecan-3-one + CO2
-
 ?
palmitoyl-CoA + L-serine SPT is the first and rate-limiting enzyme of sphingolipid biosynthesis Coccolithovirus CoA + 3-dehydro-D-sphinganine + CO2
-
 ?
palmitoyl-CoA + L-serine the viral enzyme exhibits preference for myristoyl-CoA rather than palmitoyl-CoA Coccolithovirus CoA + 3-dehydro-D-sphinganine + CO2
-
 ?

Subunits

Subunits Comment Organism
monomer single-chain enzyme, domain structure, overview Coccolithovirus

Synonyms

Synonyms Comment Organism
serine palmitoyltransferase
-
 Coccolithovirus
SPT
-
 Coccolithovirus