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Literature summary extracted from

  • Komori, H.; Nitta, Y.; Ueno, H.; Higuchi, Y.
    Structural study reveals that Ser-354 determines substrate specificity on human histidine decarboxylase (2012), J. Biol. Chem., 287, 29175-29183.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.22 expression in Escherichia coli Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.22 in complex with the inhibitor histidine methyl ester, to 1.8 A resolution. Cofactor pyridoxal 5'-phosphate is located in the large domain. The pyridine ring of pyridoxal 5'-phosphate is sandwiched between the methyl group of Ala275 and the imidazole ring of His194. Residue Ser354 is a key residue for substrate specificity Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.22 C180S/C418S mutation facilitates the purification and crystallization of enzyme. Mutant shows Km and kcat values similar to wild-type Homo sapiens
4.1.1.22 K305G complete loss of activity Homo sapiens
4.1.1.22 S354G mutation at the active site, enlarges the size of the substrate-binding pocket and results in a decreased affinity for histidine, but an acquired ability to bind and act on L-DOPA as a substrate. Mutant exhibits similar absorption spectra as wild-type with two absorption bands at 335 and 425 nm Homo sapiens
4.1.1.22 Y334F complete loss of activity Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.22 0.09
-
 L-histidine mutant C180/C418S, pH 6.8, 37°C Homo sapiens
4.1.1.22 0.1
-
 L-histidine wild-type, pH 6.8, 37°C Homo sapiens
4.1.1.22 0.13
-
 3,4-dihydroxyphenylalanine mutant S354G, pH 6.8, 37°C Homo sapiens
4.1.1.22 1.45
-
 L-histidine mutant S354G, pH 6.8, 37°C Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.22 Homo sapiens P19113
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.22 3,4-Dihydroxyphenylalanine no substrate for wild-type. Mutant S354G acquires the ability to decarboxylate 3,4-dihydroxyphenylalanine Homo sapiens Dopamine + CO2
-
 ?
4.1.1.22 L-histidine
-
 Homo sapiens histamine + CO2
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.22 1.29
-
 3,4-dihydroxyphenylalanine mutant S354G, pH 6.8, 37°C Homo sapiens
4.1.1.22 1.73
-
 L-histidine wild-type, pH 6.8, 37°C Homo sapiens
4.1.1.22 1.87
-
 L-histidine mutant C180/C418S, pH 6.8, 37°C Homo sapiens
4.1.1.22 2.01
-
 L-histidine mutant S354G, pH 6.8, 37°C Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.22 pyridoxal 5'-phosphate cofactor is located in the large domain. The pyridine ring of pyridoxal 5'-phosphate is sandwiched between the methyl group of Ala275 and the imidazole ring of His194 Homo sapiens

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.1.1.22 1.4
-
 L-histidine mutant S354G, pH 6.8, 37°C Homo sapiens
4.1.1.22 9.9
-
 3,4-dihydroxyphenylalanine mutant S354G, pH 6.8, 37°C Homo sapiens
4.1.1.22 17.3
-
 L-histidine wild-type, pH 6.8, 37°C Homo sapiens
4.1.1.22 20.8
-
 L-histidine mutant C180/C418S, pH 6.8, 37°C Homo sapiens