Literature summary for 2.5.1.61 extracted from

Bung, N.; Roy, A.; Priyakumar, U.D.; Bulusu, G.
Computational modeling of the catalytic mechanism of hydroxymethylbilane synthase (2019), Phys. Chem. Chem. Phys., 21, 7932-7940 .

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P08397	-	-

Synonyms

Synonyms	Comment	Organism
porphobilinogen deaminase	-	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
dipyrromethane	the addition of one molecule of porphobilinogen to the dipyrromethane cofactor is carried out in four steps: protonation of the substrate, porphobilinogen, deamination of porphobilinogen, electrophilic addition of the deaminated substrate to the terminal pyrrole ring of the enzyme-bound dipyrromethane cofactor and deprotonation of the carbon atom at the alpha-position of the second ring of dipyrromethane	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	the addition of one molecule of porphobilinogen to the dipyrromethane cofactor is carried out in four steps: protonation of the substrate, porphobilinogen, deamination of porphobilinogen, electrophilic addition of the deaminated substrate to the terminal pyrrole ring of the enzyme-bound dipyrromethane cofactor and deprotonation of the carbon atom at the alpha-position of the second ring of dipyrromethane. Residue R26 is proposed to be the best suitable proton donor to the porphobilinogen moiety, which aids in the deamination of the substrate. During the electrophilic addition step, the intermediate formed is stabilized by the carboxylate side chain of the D99 residue. In the final deprotonation step, an extra proton from the second ring of dipyrromethane is transferred to R26 via the carboxylate side chain of D99, thus completing one cycle of the catalytic mechanism	Homo sapiens

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Release 2023.1 (January 2023)