2.3.1.50: serine C-palmitoyltransferase
This is an abbreviated version!
For detailed information about serine C-palmitoyltransferase, go to the full flat file.
Word Map on EC 2.3.1.50
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2.3.1.50
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sphingolipids
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ceramide
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myriocin
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sphingomyelin
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sphingosine
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sphingomyelinase
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neuropathy
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sphingoid
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cholesterol
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fumonisin
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glucosylceramide
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sphingosine-1-phosphate
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3-ketodihydrosphingosine
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corneum
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glycosphingolipids
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dihydroceramide
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dihydrosphingosine
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plp-dependent
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l-cycloserine
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ormdl3
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molecular biology
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sphingomonas
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paucimobilis
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transepidermal
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charcot-marie-tooth
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analysis
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ceramide-induced
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phytosphingosine
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medicine
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asmase
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aldimine
- 2.3.1.50
- sphingolipids
- ceramide
- myriocin
- sphingomyelin
- sphingosine
- sphingomyelinase
- neuropathy
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sphingoid
- cholesterol
- fumonisin
- glucosylceramide
- sphingosine-1-phosphate
- 3-ketodihydrosphingosine
- corneum
- glycosphingolipids
- dihydroceramide
- dihydrosphingosine
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plp-dependent
- l-cycloserine
-
ormdl3
- molecular biology
- sphingomonas
- paucimobilis
-
transepidermal
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charcot-marie-tooth
- analysis
-
ceramide-induced
- phytosphingosine
- medicine
- asmase
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aldimine
Reaction
Synonyms
3-oxosphinganine synthetase, acyl-CoA:serine C-2 acyltransferase decarboxylating, LCB1, LCB2, LCB2a, LCB2b, More, palmitoyltransferase, serine, serine palmitoyl transferase, serine palmitoyltransferase, serine palmitoyltransferase 1, serine palmitoyltransferase a, serine-palmitoyl transferase, serine-palmitoyltransferase, SPT, SPT1, SPT2, SPT3, SPTase, SPTLC1, SPTLC2, ssSPT, ssSPTa, Tsc3
ECTree
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Reaction
Reaction on EC 2.3.1.50 - serine C-palmitoyltransferase
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palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
mechanism
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palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
mechanism
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palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
ordered bi-bi mechanism
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palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
formation of the external aldimine intermediate
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
using 1HNMR the exchange of the alpha-proton of L-serine with the solvent in the presence and absence of S-(2- oxoheptadecyl)-CoA, the structural analogue of palmitoyl-CoA is investagated. Results demonstrate the presence of substrate synergism, in which the alpha-proton of L-serine is activated by the binding of the second substrate palmitoyl-CoA
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
the enzyme forms a pyridoxal 5'-phosphate-L-serine-aldimine intermediate during the reaction, His159 plays multiple roles in the reaction mechanism by exploiting the stereochemistry of Dunathans conjecture. His159 promotes both the Claisen-type condensation as an acid catalyst and the protonation at Calpha of the second quinonoid to form the pyridoxal 5'-phosphate-KDS aldimine, spectral analysis, overview
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palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
the enzyme forms an external aldimine intermediate, as well as dunathan and quinoid intermediates, and followed by external beta-keto acid intermediate, and finally product quinoid and product external aldimine intermediates, reaction cycle, overview
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
the enzyme forms an external aldimine intermediate, as well as dunathan and quinoid intermediates, followed by external beta-keto acid intermediate, and finally product quinoid and product external aldimine intermediates, reaction cycle, overview
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palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
via reaction intermediate pyridoxal 5'-phosphate-L-serine aldimine, His138 changes its hydrogen bond partner from the carboxyl group of L-serine to the carbonyl group of palmitoyl-CoA upon the binding of palmitoyl-CoA, making the L-serine CaH bond perpendicular to the pyridoxal 5'-phosphate-Schiff base plane, reaction mechanism with substrate synergism in the SPT reaction, overview. Modelling of reaction intermediates
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
pyridoxal 5'-phosphate dependent reaction mechanism, key active site residues are His159, Asp231, His234, and Lys265
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
the reaction proceeds via a key carbanion/quinonoid species and an internal aldimine/PLP-bound form of the enzyme
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
the reaction proceeds via a key carbanion/quinonoid species and an internal aldimine/PLP-bound form of the enzyme
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
the reaction proceeds via several intermediate states, the pyridoxal 5'-phosphate cofactor binds to an active site lysine residue as an internal aldimine/Schiffs base (I). The L-serine displaces the lysine residue (Lys265) to form the PLP-L-serine external aldimine (II). Deprotonation of II gives a carbanion/quinonoid species (III) which condenses in a Claisen-like manner with the acyl-CoA thioester substrate to form a PLP-beta-keto acid, which then decarboxylates to generate the PLP-KDS product quinonoid (IV). This then reprotonates to form PLP-KDS aldimine (V) which is finally displaced by Lys265. The step releasing CoA and CO2 and producing the quinonoid intermediate species is irreversible. Interaction between the hydroxyl group of the L-serine substrate and the 5'-phosphate group of pyridoxal 5'-phosphate occurs in the formation of the external aldimine II, overview
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
via reaction intermediate pyridoxal 5'-phosphate-L-serine aldimine, His138 changes its hydrogen bond partner from the carboxyl group of L-serine to the carbonyl group of palmitoyl-CoA upon the binding of palmitoyl-CoA, making the L-serine CaH bond perpendicular to the pyridoxal 5'-phosphate-Schiff base plane, reaction mechanism with substrate synergism in the SPT reaction, overview. Modelling of reaction intermediates
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palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
ordered bi-bi mechanism
-
-
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
the enzyme forms an external aldimine intermediate, as well as dunathan and quinoid intermediates, and followed by external beta-keto acid intermediate, and finally product quinoid and product external aldimine intermediates, reaction cycle, overview
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