Information on EC 2.4.2.43 - lipid IVA 4-amino-4-deoxy-L-arabinosyltransferase

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The expected taxonomic range for this enzyme is: Enterobacteriaceae

EC NUMBER
COMMENTARY hide
2.4.2.43
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RECOMMENDED NAME
GeneOntology No.
lipid IVA 4-amino-4-deoxy-L-arabinosyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-amino-4-deoxy-alpha-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid A = alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[4-P-L-Ara4N]-lipid A + ditrans,octacis-undecaprenyl phosphate
show the reaction diagram
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4-amino-4-deoxy-alpha-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA = 4'-alpha-L-Ara4N-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + ditrans,octacis-undecaprenyl phosphate
show the reaction diagram
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4-amino-4-deoxy-alpha-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + lipid IVA = lipid IIA + ditrans,octacis-undecaprenyl phosphate
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
polymyxin resistance
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SYSTEMATIC NAME
IUBMB Comments
4-amino-4-deoxy-alpha-L-2-aminoarabinopyranosyl ditrans,octacis-undecaprenyl phosphate:lipid IVA L-2-aminoarabinopyranosyltransferase
Integral membrane protein present in the inner membrane of certain Gram negative endobacteria. In strains that do not produce 3-deoxy-D-manno-octulosonic acid (Kdo), the enzyme adds a single arabinose unit to the 1-phosphate moiety of the tetra-acylated lipid A precursor, lipid IVA. In the presence of a Kdo disaccharide, the enzyme primarily adds an arabinose unit to the 4-phosphate of lipid A molecules. The Salmonella typhimurium enzyme can add arabinose units to both positions.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,poly-cis-undecaprenyl phosphate + lipid IVA
lipid IIA + di-trans,poly-cis-undecaprenyl phosphate
show the reaction diagram
4-amino-4-deoxy-alpha-L-arabinopyranosyl undecaprenyl phosphate + lipid IV(A)
lipid II(A) + undecaprenyl phosphate
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,poly-cis-undecaprenyl phosphate + lipid IVA
lipid IIA + di-trans,poly-cis-undecaprenyl phosphate
show the reaction diagram
4-amino-4-deoxy-alpha-L-arabinopyranosyl undecaprenyl phosphate + lipid IV(A)
lipid II(A) + undecaprenyl phosphate
show the reaction diagram
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ArnT adds a single 4-amino-4-deoxy-alpha-L-arabinose unit to the 1-phosphate moiety of the tetraacylated lipid A precursor, lipid IV(A), which lacks Kdo and forms lipid II (A). Transfer to lipid A occurs on the periplasmic side of the inner membrane. ArnT is a bifunctional glycosyltransferase in that it can incorporate two 4-amino-4-deoxy-alpha-L-arabinose units. Lipid IV(A) = 2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose. Lipid II(A) = 2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-alpha-D-glucopyranose
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Triton X-100
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transferase—transfer of the 4-amino-4-deoxy-alpha-L-arabinose unit from its putative isoprenoid carrier, undecaprenyl phosphate-4-amino-4-deoxy-alpha-L-arabinose, to the radiolabeled acceptor [4'-32P]lipid IV(A) is dependent upon the presence of the nonionic detergent Triton X-100, with maximal activity observed at 0.2% in the assay system
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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the secondary structure of ArnT is not dependent on disulfide bridges, Salmonella typhimurium ArnT contains no disulfide bonds
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purifiation of 6*His-tagged ArnT. HisLink nickel affinity chromatography coupled with anion exchange chromatography results in the best overall purifiation strategy for dodecylmaltoside-solubilized ArnT
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overxpression of the L-Ara4N lipid A transferase (ArnT) behind a T7lac promoter
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the 6*His-tagged ArnT gene-encoded plasmids are transformed into Escherichia coli NovaBlue (Novagen) cells for protein expression. The gene is knocked out of the chromosomal DNA of BL21 (BL21(DE3)DELTAArnT), leaving the plasmid-encoded ArnT to be the only ArnT expressed in the system
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C148A/C149A/C173S/C216S/C318S/C383S/C400S/C411S
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when assayed for growth in the presence of polymyxin, the cysteine-free construct of ArnT supports growth at a level similar to that of the native protein
C148S/C149S/C173S/C216S/C318S/C383S/C400S/C411S
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mutant enzyme is inactive
C173S/C216S/C318S/C383S/C400S/C411S
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when assayed for growth in the presence of polymyxin, the cysteine-free construct of ArnT supports growth at 70% of the native protein
additional information
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analysis of 31 point mutations within a putative periplasmic loop of the cysteine-free ArnT protein, carried out using an in vivo growth assay coupled with expression studies, identification of the first time specific critical residues within the bacterial transferase. These critical residues fall into two categories: those that disrupt initial protein folding or membrane localization and those that fail to confer in vivo resistance to polymyxin despite being expressed to the inner membrane
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