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Volumn 184, Issue 19, 2002, Pages 5376-5384

Purification, substrate range, and metal center of AtzC: The N-isopropylammelide aminohydrolase involved in bacterial atrazine metabolism

Author keywords

[No Author keywords available]

Indexed keywords

AMINE; ATRAZINE; BACTERIAL PROTEIN; BENZENE DERIVATIVE; COBALT; CYANURIC ACID; FERROUS ION; GENE PRODUCT; HERBICIDE; HYDROLASE; ISOPROPYLAMINE; MANGANESE; METAL ION; N ISOPROPYLAMMELIDE AMINOHYDROLASE; NICKEL; PROTEIN ATZC; TRIAZINE; UNCLASSIFIED DRUG; ZINC ION;

EID: 0036776761     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.184.19.5376-5384.2002     Document Type: Article
Times cited : (49)

References (52)
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  • 4
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  • 23
    • 33845379666 scopus 로고
    • +2 as a probe coordination structure. 2. The ligand environment of the active site metal ion of carboxypeptidase A in ester hydrolysis
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 5225-5261
    • Kuo, L.C.1    Makinen, M.W.2
  • 51
    • 0027398949 scopus 로고
    • A pre-transition-state mimic of an enzyme: X-ray structure of adenosine deaminase with bound 1-deazaadenosine and zinc-activated water
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.