<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>8(8)</volume><submitter>Lin JF</submitter><pubmed_abstract>4-Hydroxylphenylpyruvate dioxygenase (4-HPPD) is an important enzyme for tyrosine catabolism, which catalyzes the conversion of 4-hydroxylphenylpyruvate (4-HPP) to homogentisate. In the present study, human 4-HPPD was cloned and expressed in E. coli. The kinetic parameters for 4-HPP conversion were: k cat=2.2 ± 0.1 s(-1); and K m=0.08 ± 0.02 mM. Sequence alignments show that human 4-HPPD possesses an extended C-terminus compared to other 4-HPPD enzymes. Successive truncation of the disordered tail which follows the final α-helix resulted in no changes in the K m value for 4-HPP substrate but the k cat values were significantly reduced. The results suggest that this disordered C-terminal tail plays an important role in catalysis. For inspection the effect of terminal truncation on protein s</pubmed_abstract><journal>PloS one</journal><pagination>e69733</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3739788</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>The interactions in the carboxyl terminus of human 4-hydroxyphenylpyruvate dioxygenase are critical to mediate the conformation of the final helix and the tail to shield the active site for catalysis.</pubmed_title><pmcid>PMC3739788</pmcid><pubmed_authors>Chang TC</pubmed_authors><pubmed_authors>Lin JF</pubmed_authors><pubmed_authors>Shen CP</pubmed_authors><pubmed_authors>Chang CW</pubmed_authors><pubmed_authors>Lee HJ</pubmed_authors><pubmed_authors>Chang NY</pubmed_authors><pubmed_authors>Sheih YL</pubmed_authors></additional><is_claimable>false</is_claimable><name>The interactions in the carboxyl terminus of human 4-hydroxyphenylpyruvate dioxygenase are critical to mediate the conformation of the final helix and the tail to shield the active site for catalysis.</name><description>4-Hydroxylphenylpyruvate dioxygenase (4-HPPD) is an important enzyme for tyrosine catabolism, which catalyzes the conversion of 4-hydroxylphenylpyruvate (4-HPP) to homogentisate. In the present study, human 4-HPPD was cloned and expressed in E. coli. The kinetic parameters for 4-HPP conversion were: k cat=2.2 ± 0.1 s(-1); and K m=0.08 ± 0.02 mM. Sequence alignments show that human 4-HPPD possesses an extended C-terminus compared to other 4-HPPD enzymes. Successive truncation of the disordered tail which follows the final α-helix resulted in no changes in the K m value for 4-HPP substrate but the k cat values were significantly reduced. The results suggest that this disordered C-terminal tail plays an important role in catalysis. For inspection the effect of terminal truncation on protein s</description><dates><release>2013-01-01T00:00:00Z</release><publication>2013</publication><modification>2025-04-04T19:36:06.967Z</modification><creation>2019-03-26T23:15:15Z</creation></dates><accession>S-EPMC3739788</accession><cross_references><pubmed>23950902</pubmed><doi>10.1371/journal.pone.0069733</doi></cross_references></HashMap>