Literature summary for 4.2.1.24 extracted from

Mills-Davies, N.; Butler, D.; Norton, E.; Thompson, D.; Sarwar, M.; Guo, J.; Gill, R.; Azim, N.; Coker, A.; Wood, S.; Erskine, P.; Coates, L.; Cooper, J.; Rashid, N.; Akhtar, M.; Shoolingin-Jordan, P.
Structural studies of substrate and product complexes of 5-aminolaevulinic acid dehydratase from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis (2017), Acta Crystallogr. Sect. D, 73, 9-21 .

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Activating Compound

Activating Compound	Comment	Organism	Structure
additional information	enzyme requires exogenous thiols and zinc ions for optimal activity	Pyrobaculum calidifontis

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Escherichia coli
expression in Escherichia coli	Homo sapiens
expression in Escherichia coli	Pyrobaculum calidifontis

Crystallization (Commentary)

Crystallization (Comment)	Organism
high-resolution structure of the enzyme cocrystallized with a noncovalently bound moiety of the product, porphobilinogen. The pyrrole side-chain amino group is datively bound to the active-site zinc ion and the porphobilinogen carboxylates interact with the enzyme via hydrogen bonds and salt bridges with invariant residues. Comparison of substrate and product complexes from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis	Escherichia coli
to 3.5 A resolution. Comparison of substrate and product complexes from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis	Pyrobaculum calidifontis
two monomers per asymmetric unit. In native human ALAD, the A monomer has a ligand resembling the substrate 5-aminolaevulinic acid which is covalently bound by a Schiff base to active-site Lys252 and is held in place by an ordered active-site loop. These features of the active-site structure are disordered or absent in the B subunit. Comparison of substrate and product complexes from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	requires exogenous thiols and zinc ions for optimal activity. 0.7 zinc ions per mol of subunit	Pyrobaculum calidifontis

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0ACB2	-	-
Homo sapiens	P13716	-	-
Pyrobaculum calidifontis	A3MWV9	-	-
Pyrobaculum calidifontis JCM 11548	A3MWV9	-	-

Subunits

Subunits	Comment	Organism
?	x * 37676, mass spectroscopy	Pyrobaculum calidifontis

Synonyms

Synonyms	Comment	Organism
ALAD	-	Homo sapiens
HemB	-	Escherichia coli
Pcal_1709	locus name	Pyrobaculum calidifontis

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
100	-	half-life 9 h	Pyrobaculum calidifontis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	9	-	Pyrobaculum calidifontis

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Release 2023.1 (January 2023)