A hydrogen-bonding network in mammalian sorbitol dehydrogenase stabilizes the tetrameric state and is essential for the catalytic power

Cellular and Molecular Life Sciences

Volumn 64, Issue 23, 2007, Pages 3129-3138

  Hellgren, M ^a   Kaiser, C ^a,b   De Haij, S ^a,c   Norberg, A ^a   Hoog J O ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

^b BIOVITRUM AB   (Sweden)

^c GENMAB   (Netherlands)

Author keywords

Alcohol dehydrogenase; Gibbs energy; Hydrogen bonding network; Quaternary structure; Sorbitol dehydrogenase; Structural zinc

Indexed keywords

DIMER; HYDROGEN; IDITOL DEHYDROGENASE; MONOMER; TETRAMER; TYROSINE;

ARTICLE; COMPARATIVE STUDY; COMPUTER MODEL; ELECTRICITY; ENERGY; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME SUBUNIT; EQUILIBRIUM CONSTANT; GEL FILTRATION; HUMAN; HYDROGEN BOND; IN VITRO STUDY; MAMMAL; MUTATION; NONHUMAN; RAT; TEMPERATURE; WILD TYPE;

MAMMALIA;

EID: 38549169038     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-007-7318-1     Document Type: Article

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