2006
DOI: 10.1074/jbc.m513886200
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Role for an Essential Tyrosine in Peptide Amidation

Abstract: The catalytic core of the peptidyl-␣-hydroxyglycine ␣-amidating lyase (PAL) domain of peptidylglycine ␣-amidating monooxygenase was investigated with respect to its ability to function as a ureidoglycolate lyase and the identity and role of its bound metal ions. The purified PAL catalytic core (PALcc) contains molar equivalents of calcium and zinc along with substoichiometric amounts of iron and functions as a ureidoglycolate lyase. Limiting iron availability in the cells synthesizing PALcc reduces the specifi… Show more

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Cited by 34 publications
(45 citation statements)
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“…Monofunctional SmPAL is a soluble, secreted enzyme, similar in sequence to other PALs such as the secreted Drosophila enzyme, dPAL2 [35], retaining four conserved cysteines for the maintenance of secondary structure, plus four cysteine residues unique to SmPAL, and a tyrosine residue known to be essential for functionality [39, 40]. Yet there are key amino acid substitutions in SmPAL, in the Ca 2+ binding site, and where the amino acid preceding the α-hydroxyglycine and the PAL active site interact, which set it apart from the host enzyme.…”
Section: Discussionmentioning
confidence: 99%
“…Monofunctional SmPAL is a soluble, secreted enzyme, similar in sequence to other PALs such as the secreted Drosophila enzyme, dPAL2 [35], retaining four conserved cysteines for the maintenance of secondary structure, plus four cysteine residues unique to SmPAL, and a tyrosine residue known to be essential for functionality [39, 40]. Yet there are key amino acid substitutions in SmPAL, in the Ca 2+ binding site, and where the amino acid preceding the α-hydroxyglycine and the PAL active site interact, which set it apart from the host enzyme.…”
Section: Discussionmentioning
confidence: 99%
“…The PAL domain, unique to the PAM system, is a zinc and calcium-dependent and catalyzes the dealkylation of the carbinolamide to the corresponding amide and glyoxylate (Scheme 1a). 13,14…”
Section: Introductionmentioning
confidence: 99%
“…These residues are conserved in the enzymes from C. bullatus and C. geographus . These include the four cysteine residues involved in disulfide formation, (Cys 492, 512, 559 and 570), histidine residues that coordinate a zinc ion at the active site (H444, H547, H641), or have structural roles (H393, H462) and other residues having catalytic roles (Y511, R563, D562, R394), structural roles (D449, D458, and D509) (Attenborough et al, 2012; Chufan et al, 2009; De et al, 2006; Kolhekar et al, 2002). …”
Section: Resultsmentioning
confidence: 99%