2.1.2.13: UDP-4-amino-4-deoxy-L-arabinose formyltransferase

This is an abbreviated version!
For detailed information about UDP-4-amino-4-deoxy-L-arabinose formyltransferase, go to the full flat file.

Reaction

Synonyms

ArnA, ArnA formyltransferase, ArnAFT, Pmrl

ECTree

     2 Transferases

         2.1 Transferring one-carbon groups

             2.1.2 Hydroxymethyl-, formyl- and related transferases

                2.1.2.13 UDP-4-amino-4-deoxy-L-arabinose formyltransferase

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
2507	AA Sequence
2	Application
6	Cloned(Commentary)
1	Cofactor
5	Crystallization (Commentary)
2	General Information
3	Inhibitors
6	Natural Substrates/ Products (Substrates)
10	Organism
3	Pathway
16	PDB ID
1	pH Optimum
1	Protein Variants
4	Purification (Commentary)
1	Reaction
10	Reference
11	Substrates and Products (Substrate)
2	Subunits
9	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]

Application

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Application on EC 2.1.2.13 - UDP-4-amino-4-deoxy-L-arabinose formyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide show all columns Go to Application Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

medicine

Escherichia coli

P77398

modification of the lipid A moiety of lipopolysaccharide by the addition of the sugar 4-amino-4-deoxy-L-arabinose is a strategy adopted by pathogenic Gram-negative bacteria to evade cationic antimicrobial peptides produced by the innate immune system. L-Ara4N biosynthesis is therefore a potential anti-infective target

698732

synthesis

Escherichia coli

A0A140N587

engineering of Escherichia coli to ynthesize the plant-specific flavonoid O-pentosides quercetin 3-O-xyloside and quercetin 3-O-arabinoside. For UDP-xylose biosynthesis, genes UXS (UDP-xylose synthase) from Arabidopsis thaliana and ugd (UDP-glucose dehydrogenase) from E.scherichia coli, are overexpressed. The gene encoding ArnA, which competes with UXS for UDP-glucuronic acid, is deleted. For UDP-arabinose biosynthesis, UXE (UDP-xylose epimerase) i overexpressed. UDP-dependent glycosyltransferases are engineered to ensure specificity for UDP-xylose and UDP-arabinose. The srains thus obtained synthesize approximately 160 mg/liter of quercetin 3-O-xyloside and quercetin 3-O-arabinoside

739902