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Volumn 479, Issue 2, 2008, Pages 131-138

Biochemical characterization of l-DOPA 2,3-dioxygenase, a single-domain type I extradiol dioxygenase from lincomycin biosynthesis

Author keywords

Extradiol dioxygenase; Iron ligands; l DOPA; Lincomycin; Product structure; Substrate specificity

Indexed keywords

3,4 DIHYDROXYPHENYLACETIC ACID; CATECHOL; DIHYDROCAFFEIC ACID; DIOXYGENASE; DOPA; DOPAMINE; FERROUS ION; HISTIDINE; LEVODOPA; LEVODOPA 2,3 DIOXYGENASE; LINCOMYCIN; UNCLASSIFIED DRUG;

EID: 54249095496     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2008.08.022     Document Type: Article
Times cited : (24)

References (37)
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    • ®, Microcal Software Inc., Northhampton, MA.
    • ®, Microcal Software Inc., Northhampton, MA.
  • 37
    • 54449100397 scopus 로고    scopus 로고
    • K.S. Hewitson, S.L. Holmes, D. Ehrismann, A.P. Hardy, R. Chowdhury, C.J. Schofield, M.A. McDonough, Evidence that two enzyme derived histidine ligands are sufficient for iron binding and catalysis by factor inhibiting HIF (FIH), J. Biol. Chem., 2008.
    • K.S. Hewitson, S.L. Holmes, D. Ehrismann, A.P. Hardy, R. Chowdhury, C.J. Schofield, M.A. McDonough, Evidence that two enzyme derived histidine ligands are sufficient for iron binding and catalysis by factor inhibiting HIF (FIH), J. Biol. Chem., 2008.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.