Enzyme

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     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.1 Phosphotransferases with an alcohol group as acceptor
ID:2.7.1.138
Description:Ceramide kinase.
Alternative Name: Acylsphingosine kinase.
Prosite: PDOC50146;
PDB:
PDBScop

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.1.138
BRENDA Enzyme Link: BRENDA 2.7.1.138
KEGG Enzyme Link: KEGG2.7.1.138
BioCyc Enzyme Link: BioCyc 2.7.1.138
ExPASy Enzyme Link: ExPASy2.7.1.138
EC2PDB Enzyme Link: EC2PDB 2.7.1.138
ExplorEnz Enzyme Link: ExplorEnz 2.7.1.138
PRIAM enzyme-specific profiles Link: PRIAM 2.7.1.138
IntEnz Enzyme Link: IntEnz 2.7.1.138
MEDLINE Enzyme Link: MEDLINE 2.7.1.138
MSA:

2.7.1.138;

Phylogenetic Tree:

2.7.1.138;

Uniprot:
M-CSA:
RHEA:17929 an N-acylsphing-4-enine + ATP = ADP + H(+) + N-acylsphing-4-enine 1-phosphate
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:8]-[OH;+0:7].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Synaptic vesicle ceramide kinase. A calcium-stimulated lipid kinase that co-purifies with brain synaptic vesicles.Bajjalieh SM, Martin TF, Floor E1989 Aug 252547795
A conserved cysteine motif is critical for rice ceramide kinase activity and function.Bi FC, Zhang QF, Liu Z, Fang C, Li J, Su JB, Greenberg JT, Wang HB, Yao N2011 Mar 3121483860
A lipid binding domain in sphingosine kinase 2.Don AS, Rosen H2009 Feb 2719168031
Further characterization of mammalian ceramide kinase: substrate delivery and (stereo)specificity, tissue distribution, and subcellular localization studies.Van Overloop H, Gijsbers S, Van Veldhoven PP2006 Feb16269826
MuLK, a eukaryotic multi-substrate lipid kinase.Waggoner DW, Johnson LB, Mann PC, Morris V, Guastella J, Bajjalieh SM2004 Sep 1015252046
Ceramides modulate programmed cell death in plants.Liang H, Yao N, Song JT, Luo S, Lu H, Greenberg JT2003 Nov 114563678