Mitochondrial 3β-hydroxysteroid dehydrogenase enzyme activity requires reversible pH-dependent conformational change at the intermembrane space

Journal of Biological Chemistry

Volumn 287, Issue 12, 2012, Pages 9534-9546

  Prasad, Manoj ^a   Thomas, James L ^a   Whittal, Randy M ^c   Bose, Himangshu S ^b  

^a MERCER UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b MEMORIAL HEALTH UNIVERSITY MEDICAL CENTER   (United States)

^c UNIVERSITY OF ALBERTA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONAL CHANGE; HELICAL CHARACTER; HELICAL CONTENT; HYDROXYSTEROID DEHYDROGENASE; INNER MITOCHONDRIAL MEMBRANES; INTERMEDIATE STATE; INTERMEMBRANE SPACE; ION CORES; ISOMERASE ACTIVITY; METABOLIC CONVERSION; MOLTEN GLOBULE; NATIVE STATE; PH VALUE; PH-DEPENDENT; PROTON PUMP; STOPPED-FLOW KINETICS;

CELL MEMBRANES;

MITOCHONDRIA;

3(OR 17)BETA HYDROXYSTEROID DEHYDROGENASE; GUANIDINE; PROGESTERONE;

ALPHA HELIX; ANIMAL CELL; ARTICLE; BETA SHEET; CELL MEMBRANE; CIRCULAR DICHROISM; CONCENTRATION RESPONSE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME METABOLISM; ENZYME PURIFICATION; ENZYME STRUCTURE; FLOW KINETICS; INCUBATION TIME; INTERMEMBRANE SPACE; MITOCHONDRION; MOUSE; NONHUMAN; PH; PRIORITY JOURNAL; PROGESTERONE SYNTHESIS; PROTEIN EXPRESSION; PROTEIN STABILITY; PROTEIN UNFOLDING; TITRIMETRY;

ANIMALS; CELL LINE; HUMANS; HYDROGEN-ION CONCENTRATION; KINETICS; MICE; MITOCHONDRIA; MITOCHONDRIAL MEMBRANES; PROGESTERONE REDUCTASE; PROTEIN CONFORMATION; PROTEIN FOLDING;

EID: 84863410140     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.333278     Document Type: Article

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