Conserved catalytic residues of the ALDH1L1 aldehyde dehydrogenase domain control binding and discharging of the coenzyme

Journal of Biological Chemistry

Volumn 286, Issue 26, 2011, Pages 23357-23367

  Tsybovsky, Yaroslav ^a,b   Krupenko, Sergey A ^a  

^a MEDICAL UNIVERSITY OF SOUTH CAROLINA   (United States)

^b CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

10-FORMYLTETRAHYDROFOLATE DEHYDROGENASE; ALDEHYDE DEHYDROGENASE; C-TERMINAL DOMAINS; CATALYTIC CENTER; CATALYTIC RESIDUE; COENZYME BINDING; CONFORMATIONAL CHANGE; DOUBLE MUTANTS; IRREVERSIBLE BINDING; LONG-RANGE COMMUNICATIONS; OXIDOREDUCTASES; REDOX STATE; WILD TYPES;

ALDEHYDES; AMIDES; ENZYMES; ORGANIC COMPOUNDS;

AMINO ACIDS;

ADENINE; ALANINE; ALDEHYDE DEHYDROGENASE; ALDEHYDE DEHYDROGENASE L1; CYSTEINE; FORMATE TETRAHYDROFOLATE LIGASE; GLUTAMIC ACID; NICOTINAMIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO ACID SUBSTITUTION; ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME BINDING; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN INTERACTION; WILD TYPE;

ALDEHYDE DEHYDROGENASE; AMINO ACID SUBSTITUTION; CATALYTIC DOMAIN; COENZYMES; CRYSTALLOGRAPHY, X-RAY; HUMANS; MUTATION, MISSENSE; NADP; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 79959566998     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.221069     Document Type: Article

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