HUMAN BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE

Crystal structure of human branched-chain alpha-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease.

BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE ALPHA SUBUNIT

BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE BETA SUBUNIT

SSLDDKPQFPGASAEFIDKLEFIQPNVISGIPIYRVMDRQGQIINPSEDPHLPKEKVLKLYKSMTLLNTMDRILYESQRQ
GRISFYMTNYGEEGTHVGSAAALDNTDLVFGQYREAGVLMYRDYPLELFMAQCYGNISDLGKGRQMPVHYGCKERHFVTI
SSPLATQIPQAVGAAYAAKRANANRVVICYFGEGAASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIA
ARGPGYGIMSIRVDGNDVFAVYNATKEARRRAVAENQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDHPISRLR
HYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQAERKPKPNPNLLFSDVYQEMPAQLRKQQESLARHLQTYGEHYPLDHFDK

VAHFTFQPDPEPREYGQTQKMNLFQSVTSALDNSLAKDPTAVIFGEDVAFGGVFRCTVGLRDKYGKDRVFNTPLCEQGIV
GFGIGIAVTGATAIAEIQFADYIFPAFDQIVNEAAKYRYRSGDLFNCGSLTIRSPWGCVGHGALYHSQSPEAFFAHCPGI
KVVIPRSPFQAKGLLLSCIEDKNPCIFFEPKILYRAAAEEVPIEPYNIPLSQAEVIQEGSDVTLVAWGTQVHVIREVASM
AKEKLGVSCEVIDLRTIIPWDVDTICKSVIKTGRLLISHEAPLTGGFASEISSTVQEECFLNLEAPISRVCGYDTPFPHI
FEPFYIPDKWKCYDALRKMINY

Ethanol, PEG 8000,MES, potassium chloride, magnesium chloride, glycerol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 20K

THIS IS THE E1 COMPONENT OF AN ALPHA-KETOACID DEHYDROGENASE MULTIENZYME COMPLEX. A NUMBER OF MUTATIONS HAVE BEEN CHARACTERIZED IN THIS ENZYME THAT CAUSE MAPLE SYRUP URINE DISEASE.

The biological assembly is alpha2beta2 heterotetramer with chains A and B forming one alpha subunit - the other alpha subunit symmetry partner is generated by a two-fold

The biological assembly is alpha2beta2 heterotetramer with chain C forming one beta subunit - the other beta subunit symmetry partner is generated by a two-fold

ThDP-binding fold, BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE, OXIDOREDUCTASE