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Volumn 110, Issue 3, 2000, Pages 322-329

Light-activation of NADP-malate dehydrogenase: A highly controlled process for an optimized function

Author keywords

[No Author keywords available]

Indexed keywords

CHLOROPLAST; DISULFIDE BOND; ENZYME REGULATION; ENZYME STRUCTURE; FERREDOXIN; GENETIC REGULATION; HYDROPHOBICITY; MALATE DEHYDROGENASE (NADP); PHOTOACTIVATION; TARGETED MUTAGENESIS; THIOREDOXIN;

EID: 0033676335     PISSN: 00319317     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3054.2000.1100306.x     Document Type: Short Survey
Times cited : (36)

References (53)
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    • (1983) J Biol Chem , vol.258 , pp. 472-482
    • Birktoft, J.J.1    Banaszak, L.J.2
  • 6
    • 0025923587 scopus 로고
    • 2 assimilation in oxygenic photosynthesis: The ferredoxin/thioredoxin system. Perspective on its discovery, present status and future development
    • (1991) Arch Biochem Biophys , vol.288 , pp. 1-9
    • Buchanan, B.B.1
  • 30
    • 0026726991 scopus 로고
    • Limited proteolysis of NADP-malate dehydrogenase from pea chloroplast by aminopeptidase-K yields monomers - Evidence of proteolytic degradation of NADP-malate dehydrogenase during purification from pea
    • (1993) Biochim Biophys Acta , vol.1156 , pp. 71-77
    • Kampfenkel, K.1
  • 48
  • 49
    • 84995036286 scopus 로고
    • Light/dark modulation: Regulation of chloroplast metabolism in a new light
    • (1990) Bot Acta , vol.103 , pp. 327-334
    • Scheibe, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.