2.3.1.50	acyl-CoA + L-serine	-	Homo sapiens	CoA + ?	-	?	408321	
2.3.1.50	arachidoyl-CoA + L-serine	37% activity compared to that with palmitoyl-CoA	Sphingomonas paucimobilis	CoA + 2-amino-1-hydroxydocosan-3-one + CO2	-	?	321010	
2.3.1.50	caproyl-CoA + L-serine	very low activity	Sphingomonas paucimobilis	?	-	?	455432	
2.3.1.50	elaidoyl-CoA + L-serine	39% activity compared to that with palmitoyl-CoA	Sphingomonas paucimobilis	CoA + 2-amino-1-hydroxy-trans-11-eicosen-3-one + CO2	-	?	321009	
2.3.1.50	heptadecanoyl-CoA + L-serine	-	Emiliania huxleyi	?	-	?	455758	
2.3.1.50	heptadecanoyl-CoA + L-serine	less than 50% activity compared to palmitoyl-CoA	Emiliania huxleyi virus sp.	?	-	?	455758	
2.3.1.50	heptadecanoyl-CoA + L-serine	less than 50% activity compared to palmitoyl-CoA	Emiliania huxleyi virus sp. 201	?	-	?	455758	
2.3.1.50	heptadecanoyl-CoA + L-serine	-	Emiliania huxleyi CCMP374	?	-	?	455758	
2.3.1.50	L-alanine + palmitoyl-CoA	-	Homo sapiens	CoA + (2S)-2-aminooctadecan-3-one + CO2	-	?	420822	
2.3.1.50	L-alanine + stearoyl-CoA	-	Homo sapiens	CoA + (2S)-2-aminoicosan-3-one + CO2	-	?	420824	
2.3.1.50	L-serine + palmitoyl-CoA	-	Homo sapiens	CoA + 3-dehydro-D-sphinganine + CO2	-	?	420885	
2.3.1.50	L-serine + palmitoyl-CoA	-	Sphingomonas paucimobilis	CoA + 3-dehydro-D-sphinganine + CO2	-	?	420885	
2.3.1.50	L-serine + stearoyl-CoA	-	Homo sapiens	CoA + (2S)-2-amino-1-hydroxyicosan-3-one + CO2	-	?	420887	
2.3.1.50	lauroyl-CoA + L-serine	18% activity compared to that with palmitoyl-CoA	Sphingomonas paucimobilis	CoA + 2-amino-1-hydroxytetradecan-3-one + CO2	-	?	321011	
2.3.1.50	lauroyl-CoA + L-serine	18% activity compared to palmitoyl-CoA	Sphingomonas paucimobilis	CoA + 2-amino-1-hydroxytetradecan-3-one + CO2	-	?	321011	
2.3.1.50	additional information	specificity	Rattus norvegicus	?	-	?	89	
2.3.1.50	additional information	increasing the acyl-CoA chain length above C16 by 1 or 2 carbons is less detrimental to activity than similar decrements in chain length	Homo sapiens	?	-	?	89	
2.3.1.50	additional information	44% reduction of SPT activity in patiens with hereditary sensory neuropathy type I with mutation T399G in the SPTLC1 gene. However the decrease in SPT activity has no effect on de novo sphingolipid biosynthesis, cellular sphingolipid content, cell proliferation and death. Despite the inhibition of mutant allele, the activity of nonmutant allele of SPT may be sufficient for adequate sphingolipid biosynthesis and cell viability. The neurodegeneration in HSN1 is likely to be caused by subtler and rather long-term effects of these mutations such as loss of a cell-type selective facet of sphingolipid metabolism and/or function, or perhaps accumulation of toxic species, including abnormal proteins	Homo sapiens	?	-	?	89	
2.3.1.50	additional information	elevation of ceramide in serum lipoproteins during acute phase response to inflammation is accompanied by activation of serine-palmitoyl transferase in liver	Mus musculus	?	-	?	89	
2.3.1.50	additional information	elevation of ceramide in serum lipoproteins during acute phase response to inflammation is accompanied by activation of serine-palmitoyl transferase in liver	Homo sapiens	?	-	?	89	
2.3.1.50	additional information	mutations in the enzyme subunit SPTLC1 cause hereditary sensory and autonomic neuropathy type I, HSAN1, an adult onset, autosomal dominant neuropathy, HSAN1 patients have reduced SPT activity, link between mutant SPT and neuronal dysfunction	Homo sapiens	?	-	?	89	
2.3.1.50	additional information	stearoyl-CoA desaturase-1 deficiency, SCD1 deficiency, reduces ceramide synthesis by downregulating SPT and increasing beta-oxidation in skeletal muscle	Mus musculus	?	-	?	89	
2.3.1.50	additional information	the enzyme activity and expression in the heart is not affected by high-fat feeding	Rattus norvegicus	?	-	?	89	
2.3.1.50	additional information	the expression of two SPT isoforms could be a cellular mechanism to adjust SPT activity to tissue-specific requirements of sphingolipid synthesis	Homo sapiens	?	-	?	89	
2.3.1.50	additional information	the viral single-chain enzyme might form multiprotein complexes in vivo with functions different from the monomer	Coccolithovirus	?	-	?	89	
2.3.1.50	additional information	acyl-CoA substrate specificity, overview	Coccolithovirus	?	-	?	89	
2.3.1.50	additional information	the LCB2 subunit of the sphingolipid biosynthesis enzyme SPT can function as an attenuator of the hypersensitive response and Bax-induced cell death, overview	Brassica rapa subsp. oleifera	?	-	?	89	
2.3.1.50	additional information	ability of the ssSPT subunits to modulate the chain lengths of LCBs in mammalian cells	Homo sapiens	?	-	?	89	
2.3.1.50	additional information	assay optimization measuring radio-labeled L-serine incorporation into 3-oxodihydrosphingosine in microsomes or crude cell lysate, usage of an nonradioactive HPLC-based detection protocol, overview	Homo sapiens	?	-	?	89	
2.3.1.50	additional information	1-deoxysphingolipids are atypical sphingolipids that are formed by the enzyme serine palmitoyltransferase due to a promiscuous use of L-alanine over its canonical substrate L-serine. Wild-type SPT forms 1-deoxysphingolipids under certain conditions, and elevated levels are found in individuals with the metabolic syndrome and diabetes	Homo sapiens	?	-	?	89	
2.3.1.50	additional information	the small subunit of serine palmitoyltransferase a (ssSPTa) as an lysophosphatidylinositol acyltransferase 1 (LPIAT1)-interacting protein	Homo sapiens	?	-	?	89	
2.3.1.50	additional information	no activity with L-phosphoserine	Sphingomonas paucimobilis	?	-	?	89	
2.3.1.50	additional information	no activity with octanoyl-CoA	Sphingomonas paucimobilis	?	-	-	89	
2.3.1.50	myristoleoyl-CoA + L-serine	46% activity compared to that with palmitoyl-CoA	Sphingomonas paucimobilis	CoA + 2-amino-1-hydroxy-cis-11-hexadecen-3-one + CO2	-	?	321008	
2.3.1.50	myristoyl-CoA + L-serine	-	Rattus norvegicus	CoA + 2-amino-1-hydroxyhexadecan-3-one + CO2	-	?	321005	
2.3.1.50	myristoyl-CoA + L-serine	second best substrate	Sphingomonas paucimobilis	CoA + 2-amino-1-hydroxyhexadecan-3-one + CO2	-	?	321005	
2.3.1.50	myristoyl-CoA + L-serine	75% activity compared to that with palmitoyl-CoA	Sphingomonas paucimobilis	CoA + 2-amino-1-hydroxyhexadecan-3-one + CO2	-	?	321005	
2.3.1.50	myristoyl-CoA + L-serine	SPT is the first and rate-limiting enzyme of sphingolipid biosynthesis	Coccolithovirus	CoA + 2-amino-1-hydroxyhexadecan-3-one + CO2	-	?	321005	
2.3.1.50	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	-	?	321005	
2.3.1.50	myristoyl-CoA + L-serine	75% activity compared to that with palmitoyl-CoA	Sphingomonas paucimobilis EY2395	CoA + 2-amino-1-hydroxyhexadecan-3-one + CO2	-	?	321005	
2.3.1.50	myristoyl-CoA + L-serine	-	Homo sapiens	CoA + ? + CO2	-	?	407278	
2.3.1.50	myristoyl-CoA + L-serine	recombinant SPTLC3 subunit in HEK-293 cells	Homo sapiens	CoA + ? + CO2	-	?	407278	
2.3.1.50	myristoyl-CoA + L-serine	-	Emiliania huxleyi	?	-	?	456035	
2.3.1.50	myristoyl-CoA + L-serine	less than 50% activity compared to palmitoyl-CoA	Emiliania huxleyi virus sp.	?	-	?	456035	
2.3.1.50	myristoyl-CoA + L-serine	less than 50% activity compared to palmitoyl-CoA	Emiliania huxleyi virus sp. 201	?	-	?	456035	
2.3.1.50	myristoyl-CoA + L-serine	-	Emiliania huxleyi CCMP374	?	-	?	456035	
2.3.1.50	n-heptadecanoyl-CoA + L-serine	75% activity compared to that with palmitoyl-CoA	Sphingomonas paucimobilis	CoA + 2-amino-1-hydroxynonadecan-3-one + CO2	-	?	321004	
2.3.1.50	n-heptadecanoyl-CoA + L-serine	75% activity compared to that with palmitoyl-CoA	Sphingomonas paucimobilis EY2395	CoA + 2-amino-1-hydroxynonadecan-3-one + CO2	-	?	321004	
2.3.1.50	oleoyl-CoA + L-serine	57% activity compared to that with palmitoyl-CoA	Sphingomonas paucimobilis	CoA + 2-amino-1-hydroxy-11-cis-eicosen-3-one + CO2	-	?	321006	
2.3.1.50	palmitoleoyl-CoA + L-serine	80% activity compared to that with palmitoyl-CoA	Sphingomonas paucimobilis	CoA + 2-amino-1-hydroxy-cis-11-octadecen-3-one + CO2	-	?	321003	
2.3.1.50	palmitoleoyl-CoA + L-serine	80% activity compared to that with palmitoyl-CoA	Sphingomonas paucimobilis EY2395	CoA + 2-amino-1-hydroxy-cis-11-octadecen-3-one + CO2	-	?	321003	
2.3.1.50	palmitoyl-CoA + L-alanine	wild-type enzyme can metabolize L-alanine under certain conditions	Homo sapiens	CoA + (2S)-2-aminooctadecan-3-one + CO2	-	?	434711	
2.3.1.50	palmitoyl-CoA + L-alanine	low activity with the wild-type enzyme, but increased activity with some mutants of the enzyme, overview	Homo sapiens	CoA + (2S)-2-aminooctadecan-3-one + CO2	-	?	434711	
2.3.1.50	palmitoyl-CoA + L-serine	-	Cricetulus griseus	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	-	Mus musculus	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	-	Homo sapiens	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	-	Rattus norvegicus	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	-	Rattus norvegicus	CoA + 3-dehydro-D-sphinganine + CO2	-	ir	321002	
2.3.1.50	palmitoyl-CoA + L-serine	-	Saccharomyces cerevisiae	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	-	Saccharomyces cerevisiae	CoA + 3-dehydro-D-sphinganine + CO2	-	ir	321002	
2.3.1.50	palmitoyl-CoA + L-serine	-	Arabidopsis thaliana	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	-	Sphingomonas paucimobilis	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	-	Cucurbita pepo	CoA + 3-dehydro-D-sphinganine + CO2	-	ir	321002	
2.3.1.50	palmitoyl-CoA + L-serine	-	Wickerhamomyces ciferrii	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	-	Wickerhamomyces ciferrii	CoA + 3-dehydro-D-sphinganine + CO2	-	ir	321002	
2.3.1.50	palmitoyl-CoA + L-serine	-	Prevotella melaninogenica	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	-	Prevotella melaninogenica	CoA + 3-dehydro-D-sphinganine + CO2	-	ir	321002	
2.3.1.50	palmitoyl-CoA + L-serine	-	Emiliania huxleyi	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	-	Homo sapiens	CoA + 3-dehydro-D-sphinganine + CO2	-	ir	321002	
2.3.1.50	palmitoyl-CoA + L-serine	-	Sphingobacterium multivorum	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	-	Sphingobacterium spiritivorum	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	-	Bacteriovorax stolpii	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	-	Canis lupus familiaris	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	-	Emiliania huxleyi virus sp.	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	-	Rattus norvegicus	CoA + 3-dehydro-D-sphinganine + CO2	i.e. 2-amino-1-hydroxyoctadecane-3-one, i.e. 3-oxo-dihydroxysphingosine	ir	321002	
2.3.1.50	palmitoyl-CoA + L-serine	-	Wickerhamomyces ciferrii	CoA + 3-dehydro-D-sphinganine + CO2	i.e. 2-amino-1-hydroxyoctadecane-3-one, i.e. 3-oxo-dihydroxysphingosine	ir	321002	
2.3.1.50	palmitoyl-CoA + L-serine	100% activity	Sphingomonas paucimobilis	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	100% activity	Emiliania huxleyi virus sp.	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	palmitoyl-CoA is the preferred substrate	Rattus norvegicus	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	palmitoyl-CoA is the preferred substrate	Rattus norvegicus	CoA + 3-dehydro-D-sphinganine + CO2	-	ir	321002	
2.3.1.50	palmitoyl-CoA + L-serine	palmitoyl-CoA is the preferred substrate	Sphingomonas paucimobilis	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	palmitoyl-CoA is the preferred substrate	Cucurbita pepo	CoA + 3-dehydro-D-sphinganine + CO2	-	ir	321002	
2.3.1.50	palmitoyl-CoA + L-serine	optimal palmitoyl-CoA concentration is 0.2 mM	Cucurbita pepo	CoA + 3-dehydro-D-sphinganine + CO2	-	ir	321002	
2.3.1.50	palmitoyl-CoA + L-serine	activities are greatest with palmitoyl-CoA and palmitelaidoyl-CoA, followed by fully saturated homologs, activity considerably diminishes as the alkyl-chain length increases or decreases, or with the presence of a cis-double bond	Rattus norvegicus	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	no other amino acids can substitute for serine	Rattus norvegicus	CoA + 3-dehydro-D-sphinganine + CO2	-	ir	321002	
2.3.1.50	palmitoyl-CoA + L-serine	no other amino acids can substitute for serine	Sphingomonas paucimobilis	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	palmitoyl-CoA is used in preference to other saturated or unsaturated acyl-CoA substrates	Homo sapiens	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	palmitoyl-CoA is used in preference to other saturated or unsaturated acyl-CoA substrates	Cucurbita pepo	CoA + 3-dehydro-D-sphinganine + CO2	-	ir	321002	
2.3.1.50	palmitoyl-CoA + L-serine	involved in cellular stress response	Homo sapiens	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	involved in cellular stress response	Saccharomyces cerevisiae	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	first step of biosynthesis of sphingolipid bases	Cricetulus griseus	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	first step of biosynthesis of sphingolipid bases	Mus musculus	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	first step of biosynthesis of sphingolipid bases	Homo sapiens	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	first step of biosynthesis of sphingolipid bases	Rattus norvegicus	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	first step of biosynthesis of sphingolipid bases	Rattus norvegicus	CoA + 3-dehydro-D-sphinganine + CO2	-	ir	321002	
2.3.1.50	palmitoyl-CoA + L-serine	first step of biosynthesis of sphingolipid bases	Saccharomyces cerevisiae	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	first step of biosynthesis of sphingolipid bases	Wickerhamomyces ciferrii	CoA + 3-dehydro-D-sphinganine + CO2	-	ir	321002	
2.3.1.50	palmitoyl-CoA + L-serine	rate-limiting enzyme in synthesis of sphingolipids	Homo sapiens	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	rate-limiting enzyme in synthesis of sphingolipids	Saccharomyces cerevisiae	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	rate-limiting enzyme in synthesis of sphingolipids	Sphingomonas paucimobilis	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	initial step of de novo ceramide biosynthesis	Homo sapiens	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	initial step of de novo ceramide biosynthesis	Rattus norvegicus	CoA + 3-dehydro-D-sphinganine + CO2	-	ir	321002	
2.3.1.50	palmitoyl-CoA + L-serine	initial step of de novo ceramide biosynthesis	Saccharomyces cerevisiae	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	initial step of de novo ceramide biosynthesis	Saccharomyces cerevisiae	CoA + 3-dehydro-D-sphinganine + CO2	-	ir	321002	
2.3.1.50	palmitoyl-CoA + L-serine	initial step of de novo ceramide biosynthesis	Prevotella melaninogenica	CoA + 3-dehydro-D-sphinganine + CO2	-	ir	321002	
2.3.1.50	palmitoyl-CoA + L-serine	key enzyme of sphingolipid metabolism	Cricetulus griseus	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	the enzyme catalyzes the initial and rate-limiting step in de novo sphingolipid synthesis. Potential role for overexpression of SPT in processes of cell metastasis	Homo sapiens	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	key enzyme in ceramide synthesis, overview	Mus musculus	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	SPT is the first and rate-limiting enzyme of sphingolipid biosynthesis	Coccolithovirus	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	step in the sphingolipid biosynthetic pathway, overview	Arabidopsis thaliana	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	the enzyme catalyses the first step in the ceramide biosynthesis pathway	Rattus norvegicus	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	the enzyme catalyses the rate limiting step for the de novo synthesis of sphingolipids	Cricetulus griseus	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	the enzyme catalyses the rate limiting step for the de novo synthesis of sphingolipids	Homo sapiens	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	the enzyme catalyses the rate limiting step for the de novo synthesis of sphingolipids, the dynamic composition of the SPT complex could provide a cellular mechanism to adjust SPT activity to tissue specific requirements in sphingolipid synthesis	Homo sapiens	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	the enzyme is involved in the ceramide metabolism, overview	Rattus norvegicus	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	the viral enzyme exhibits preference for myristoyl-CoA rather than palmitoyl-CoA	Coccolithovirus	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	first and rate-limiting step in the de novo synthesis of sphingolipids	Homo sapiens	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	His159 is the anchoring site for L-serine and regulates the alpha-deprotonation of L-serine by fixing the conformation of the pyridoxal 5'-phosphate-L-serine aldimine to prevent unwanted side reactions	Sphingomonas paucimobilis	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	interaction between the hydroxyl group of the L-serine substrate and the 5'-phosphate group of pyridoxal 5'-phosphate. This interaction is important for substrate specificity and optimal catalytic efficiency	Sphingomonas paucimobilis	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	-	Emiliania huxleyi virus sp. 201	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	100% activity	Emiliania huxleyi virus sp. 201	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	-	Emiliania huxleyi CCMP374	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	-	Rattus norvegicus Sprague Dawley	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	-	Sphingobacterium multivorum GTC97	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	palmitoyl-CoA is the preferred substrate	Sphingomonas paucimobilis EY2395	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	no other amino acids can substitute for serine	Sphingomonas paucimobilis EY2395	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	-	Sphingomonas paucimobilis EY2395	CoA + 3-dehydro-D-sphinganine + CO2	-	?	321002	
2.3.1.50	palmitoyl-CoA + L-serine	-	Rhizorhabdus wittichii	3-dehydrosphinganine + CoA + CO2	-	?	421167	
2.3.1.50	palmitoyl-CoA + [1,2,3-13C,2-15N] L-serine	-	Sphingomonas paucimobilis	?	-	?	456209	
2.3.1.50	palmitoyl-CoA + [1,2,3-13C,2-15N] L-serine	-	Homo sapiens	?	-	?	456209	
2.3.1.50	palmitoyl-CoA + [2,3,3-D] L-serine	-	Sphingomonas paucimobilis	?	-	?	456210	
2.3.1.50	palmitoyl-CoA + [2,3,3-D] L-serine	-	Homo sapiens	?	-	?	456210	
2.3.1.50	palmitoyl-CoA + [2-13C] L-serine	-	Sphingomonas paucimobilis	?	-	?	456211	
2.3.1.50	palmitoyl-CoA + [2-13C] L-serine	-	Homo sapiens	?	-	?	456211	
2.3.1.50	palmitoyl-CoA + [3,3-D] L-serine	-	Sphingomonas paucimobilis	?	-	?	456212	
2.3.1.50	palmitoyl-CoA + [3,3-D] L-serine	-	Homo sapiens	?	-	?	456212	
2.3.1.50	pentadecanoyl-CoA + L-serine	-	Emiliania huxleyi	?	-	?	454459	
2.3.1.50	pentadecanoyl-CoA + L-serine	less than 50% activity compared to palmitoyl-CoA	Emiliania huxleyi virus sp.	?	-	?	454459	
2.3.1.50	pentadecanoyl-CoA + L-serine	less than 50% activity compared to palmitoyl-CoA	Emiliania huxleyi virus sp. 201	?	-	?	454459	
2.3.1.50	pentadecanoyl-CoA + L-serine	-	Emiliania huxleyi CCMP374	?	-	?	454459	
2.3.1.50	S-(2-oxoheptadecyl)-CoA + L-serine	-	Sphingomonas paucimobilis	CoA + ?	-	?	398263	
2.3.1.50	S-(2-oxoheptadecyl)-CoA + L-serine	-	Homo sapiens	CoA + ?	-	?	398263	
2.3.1.50	stearoyl-CoA + L-serine	51% activity compared to that with palmitoyl-CoA	Sphingomonas paucimobilis	CoA + 2-amino-1-hydroxyeicosan-3-one + CO2	-	?	321007	
2.3.1.50	stearoyl-CoA + L-serine	-	Rhizorhabdus wittichii	(2S)-2-amino-1-hydroxyicosan-3-one + CoA + CO2	-	?	421525	
2.3.1.50	stearoyl-CoA + L-serine	-	Homo sapiens	CoA + (2S)-2-amino-1-hydroxyicosan-3-one + CO2	-	?	435836	
2.3.1.50	stearoyl-CoA + L-serine	-	Rattus norvegicus	CoA + (2S)-2-amino-1-hydroxyicosan-3-one + CO2	-	?	435836