To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS.
To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017.
From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...]
View this page in https

ENZYME entry: EC 2.4.99.15

Accepted Name
(Kdo)(3)-lipid IV(A) (2-4) 3-deoxy-D-manno-octulosonic acid transferase.
Alternative Name(s)
3-deoxy-D-manno-oct-2-ulosonic acid transferase.
3-deoxy-manno-octulosonic acid transferase.
Kdo transferase.
Reaction catalysed
Alpha-Kdo-(2->8)-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IV(A) + CMP-beta-Kdo <=> alpha-Kdo-(2->8)-(alpha-Kdo-(2->4))-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IV(A) + CMP
Comment(s)
The enzyme from Chlamydia psittaci transfers four KDO residues to lipid A, forming a branched tetrasaccharide with the structure alpha- KDO-(2,8)-(alpha-KDO-(2,4))-alpha-KDO-(2,4)-alpha-KDO (cf. EC 2.4.99.12, EC 2.4.99.13 and EC 2.4.99.14).
Cross-references
BRENDA2.4.99.15
EC2PDB2.4.99.15
ExplorEnz2.4.99.15
PRIAM enzyme-specific profiles2.4.99.15
KEGG Ligand Database for Enzyme Nomenclature2.4.99.15
IUBMB Enzyme Nomenclature2.4.99.15
IntEnz2.4.99.15
MEDLINEFind literature relating to 2.4.99.15
MetaCyc2.4.99.15
UniProtKB/Swiss-Prot
F0T4D1, KDTA_CHLP6

View entry in original ENZYME format
View entry in raw text format (no links)

All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.4.99.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.4.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.-.-.-