EC number:2.7.1.14

Enzyme

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EC Tree
     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.1 Phosphotransferases with an alcohol group as acceptor
ID:2.7.1.14
Description:Sedoheptulokinase.
Alternative Name: Heptulokinase.
Cath: 3.30.420.40;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.1.14
BRENDA Enzyme Link: BRENDA 2.7.1.14
KEGG Enzyme Link: KEGG2.7.1.14
BioCyc Enzyme Link: BioCyc 2.7.1.14
ExPASy Enzyme Link: ExPASy2.7.1.14
EC2PDB Enzyme Link: EC2PDB 2.7.1.14
ExplorEnz Enzyme Link: ExplorEnz 2.7.1.14
PRIAM enzyme-specific profiles Link: PRIAM 2.7.1.14
IntEnz Enzyme Link: IntEnz 2.7.1.14
MEDLINE Enzyme Link: MEDLINE 2.7.1.14

EC number:2.7.1.14

MSA:

2.7.1.14;
Phylogenetic Tree:

2.7.1.14;
Uniprot:
M-CSA:
RHEA:23844 ATP + sedoheptulose = ADP + D-sedoheptulose 7-phosphate + H(+)
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
The sedoheptulose kinase CARKL directs macrophage polarization through control of glucose metabolism.Haschemi A, Kosma P, Gille L, Evans CR, Burant CF, Starkl P, Knapp B, Haas R, Schmid JA, Jandl C, Amir S, Lubec G, Park J, Esterbauer H, Bilban M, Brizuela L, Pospisilik JA, Otterbein LE, Wagner O2012 Jun 622682222
Sedoheptulokinase deficiency due to a 57-kb deletion in cystinosis patients causes urinary accumulation of sedoheptulose: elucidation of the CARKL gene.Wamelink MM, Struys EA, Jansen EE, Levtchenko EN, Zijlstra FS, Engelke U, Blom HJ, Jakobs C, Wevers RA2008 Apr18186520