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

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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gatzeva-Topalova, P.Z.; May, A.P.; Sousa, M.C.
Crystal structure and mechanism of the Escherichia coli ArnA (PmrI) transformylase domain. An enzyme for lipid A modification with 4-amino-4-deoxy-L-arabinose and polymyxin resistance
Biochemistry
44
5328-5338
2005
Escherichia coli (P77398)
Manually annotated by BRENDA team
Breazeale, S.D.; Ribeiro, A.A.; Raetz, C.R.
Oxidative decarboxylation of UDP-glucuronic acid in extracts of polymyxin-resistant Escherichia coli. Origin of lipid a species modified with 4-amino-4-deoxy-L-arabinose
J. Biol. Chem.
277
2886-2896
2001
Escherichia coli (P77398)
Manually annotated by BRENDA team
Breazeale, S.D.; Ribeiro, A.A.; McClerren, A.L.; Raetz, C.R.
A formyltransferase required for polymyxin resistance in Escherichia coli and the modification of lipid A with 4-Amino-4-deoxy-L-arabinose. Identification and function oF UDP-4-deoxy-4-formamido-L-arabinose
J. Biol. Chem.
280
14154-14167
2005
Escherichia coli
Manually annotated by BRENDA team
Williams, G.J.; Breazeale, S.D.; Raetz. C.R.; Naismith. J.H.
Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis
J. Biol. Chem.
280
23000-23008
2005
Escherichia coli (P77398)
Manually annotated by BRENDA team
Gatzeva-Topalova, P.Z.; May, A.P.; Sousa, M.C.
Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance.
Structure
13
929-942
2005
Escherichia coli (P77398)
Manually annotated by BRENDA team
Fischer, U.; Hertlein, S.; Grimm, C.
The structure of apo ArnA features an unexpected central binding pocket and provides an explanation for enzymatic cooperativity
Acta Crystallogr. Sect. D
71
687-696
2015
Escherichia coli (P77398)
Manually annotated by BRENDA team
Han, S.H.; Kim, B.G.; Yoon, J.A.; Chong, Y.; Ahn, J.H.
Synthesis of flavonoid O-pentosides by Escherichia coli through engineering of nucleotide sugar pathways and glycosyltransferase
Appl. Environ. Microbiol.
80
2754-2762
2014
Escherichia coli (A0A140N587)
Manually annotated by BRENDA team