2.4.99.13: (Kdo)-lipid IVA 3-deoxy-D-manno-octulosonic acid transferase
This is an abbreviated version!
For detailed information about (Kdo)-lipid IVA 3-deoxy-D-manno-octulosonic acid transferase, go to the full flat file.
Reaction
Synonyms
(KDO)-lipid IVA 3-deoxy-D-manno-octulosonic acid transferase, 3-deoxy-D-manno-2-octulosonic acid transferase, 3-deoxy-D-manno-oct-2-ulosonic acid transferase, 3-deoxy-D-manno-oct-2-ulosonic acid transferases, 3-deoxy-D-manno-octulosonic acid transferase, 3-deoxy-manno-octulosonic acid transferase, CMP-3-deoxy-D-manno-oct-2-ulosonate:(Kdo)-lipid IVA 3-deoxy-D-manno-oct-2-ulosonate transferase, Kdo transferase, KdtA, multi-functional Kdo-transferase, WaaA
ECTree
2.4.99.13 (Kdo)-lipid IVA 3-deoxy-D-manno-octulosonic acid transferaseAdvanced search results
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General Information on EC 2.4.99.13 - (Kdo)-lipid IVA 3-deoxy-D-manno-octulosonic acid transferase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
malfunction
metabolism
the enzyme is involved in the synthesis of a mitochondrial not yet identified lipid A-like molecule rather than in the synthesis of the cell wall rhamnogalacturonan II
physiological function
malfunction
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construction of a kdtA::kan insertion mutation, using a gene replacement method. Growth of this strain is absolutely dependent upon the presence of a functional copy of the kdtA gene (or the related gseA gene) carried on a plasmid
malfunction
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kdtA deletion mutants are viable when lpxL and lpxM (the lauroyl- or the myristoyltransferase of lipid A biosynthesis) are overexpressed. Deletion of kdtA in strains overexpressing LpxM causes accumulation of pentaacylated lipid A with a secondary myristate moiety. None of the strains lacking kdtA grow in the presence of bile salts at any temperature or on nutrient broth at 42°C
malfunction
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waaA (monofunctional Kdo transferase) of Haemophilus influenzae can not complement a knockout mutation in the corresponding gene of an Re-type Escherichia coli strain (encoding a bifunctional enzyme that transfers two 3-deoxy-D-manno-octulosonate residues to the lipid A precursor). However, complementation is possible by coexpressing the recombinant waaA together with the LPS-specific KDO kinase gene (kdkA) of Haemophilus influenzae DSM11121 or I69, respectively
physiological function
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chlamydial KDO transferases can replace in Escherichia coli K-12 the host's KDO transferase and retain the product specificities described in their natural background. WaaA from Chlamydia psittaci transfers predominantly 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
physiological function
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the main function of Kdo transferase is to provide the right substrates for the acyltransferases LpxL and LpxM, resulting in the synthesis of penta- and hexaacylated lipid A, which is optimal for the MsbA flippase
physiological function
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chlamydial KDO transferases can replace in Escherichia coli K-12 the host's KDO transferase and retain the product specificities described in their natural background. WaaA from Chlamydia psittaci transfers predominantly 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
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