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Volumn 46, Issue 3, 2002, Pages 321-329

Structure and cooperativity of a T-state mutant of histidine decarboxylase from Lactobacillus 30a

Author keywords

Cooperativity; Enzyme activation; Helix disorder; Histidine decarboxylase; Mutation

Indexed keywords

HISTAMINE; HISTIDINE; HISTIDINE DECARBOXYLASE;

EID: 0037083392     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10042     Document Type: Conference Paper
Times cited : (7)

References (28)
  • 19
    • 84944812409 scopus 로고
    • Improved fourier coefficients for maps using phases from partial structures with errors
    • (1986) Acta Crystallogr A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 22
    • 0030498233 scopus 로고    scopus 로고
    • xdlMAPMAN and xdlDATAMAN - Programs for reformatting, analysis, and manipulation of biomolecular electron-density maps and reflection data sets
    • (1996) Acta Crystallogr D , vol.5 , pp. 826-828
    • Kleywegt, G.J.1    Jones, T.A.2
  • 25
    • 0023003495 scopus 로고
    • Pyruvoyl-dependent histidine decarboxylase from Lactobacillus 30a. Covalent modifications of aspartic acid 191, lysine 155, and the pyruvoyl group
    • (1986) J Biol Chem , vol.261 , pp. 4389-4394
    • Huynh, Q.K.1    Snell, E.E.2
  • 28


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.