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Reference on EC 4.1.1.19 - arginine decarboxylase and Organism(s) Yersinia pestis and UniProt Accession Q8ZHG8

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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Balbo, P.B.; Patel, C.N.; Sell, K.G.; Adcock, R.S.; Neelakantan, S.; Crooks, P.A.; Oliveira, M.A.
Spectrophotometric and steady-state kinetic analysis of the biosynthetic arginine decarboxylase of Yersinia pestis utilizing arginine analogues as inhibitors and alternative substrates
Biochemistry
42
15189-15196
2003
Yersinia pestis
Manually annotated by BRENDA team
Patel, C.N.; Adcock, R.S.; Sell, K.G.; Oliveira, M.A.
Crystallization, X-ray diffraction and oligomeric characterization of arginine decarboxylase from Yersinia pestis, a key polyamine biosynthetic enzyme
Acta Crystallogr. Sect. D
60
2396-2398
2004
Yersinia pestis
Manually annotated by BRENDA team
Counts, K.G.; Wong, I.; Oliveira, M.A.
Investigating the geminal diamine intermediate of Yersinia pestis arginine decarboxylase with substrate, product, and inhibitors using single wavelength stopped-flow spectroscopy
Biochemistry
46
379-386
2007
Yersinia pestis (Q8ZHG8), Yersinia pestis
Manually annotated by BRENDA team