Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Dopamine inhibition of human tyrosine hydroxylase type 1 is controlled by the specific portion in the N-terminus of the enzyme.

Journal of neurochemistry - 1 May 1999

Nakashima A, Mori K, Suzuki T, Kurita H, Otani M, Nagatsu T, Ota A

Abstract excerpt

Tyrosine hydroxylase (TH), which converts L-tyrosine to L-DOPA, is a rate-limiting enzyme in the biosynthesis of catecholamines; its activity is regulated by feedback inhibition by catecholamine products including dopamine. To investigate the specific portion of the N-terminus of TH that determines the efficiency of dopamine inhibition, wild-type and N-terminal 35-, 38-, and 44-amino acid-deleted mutants (del-35,...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Catalysis
Share to Dopamine
Share to Iron

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Isoenzymes

Share to Kinetics

Share to Peptide Fragments

Share to Recombinant Proteins

Share to Tyrosine 3-Monooxygenase

Source

Identifiers

PMID: 10217296
DOI: 10.1046/j.1471-4159.1999.0722145.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Dopamine inhibition of human tyrosine hydroxylase type 1 is controlled by the specific portion in the N-terminus of the enzyme.PMID 10217296Read ↗

Positive charge intrinsic to Arg(37)-Arg(38) is critical for dopamine inhibition of the catalytic activity of human tyrosine hydroxylase type 1.Semantic proximity Read ↗

The Structure of Human Tyrosine Hydroxylase Reveals the Mechanism for Feedback Inhibition by DopamineSemantic proximity Read ↗

Recessively inherited L-DOPA-responsive dystonia caused by a point mutation (Q381K) in the tyrosine hydroxylase gene.Semantic proximity Read ↗

Tetrahydrobiopterin (BH4) treatment stabilizes tyrosine hydroxylase: Rescue of tyrosine hydroxylase deficiency phenotypes in human neurons and in a knock-in mouse model.Semantic proximity Read ↗

Tyrosine hydroxylase activity is regulated through the modification of the 176th cysteine residue.Semantic proximity Read ↗

Catecholamine biosynthesis and physiological regulation in neuroendocrine cells.Semantic proximity Read ↗

Divergence in enzyme regulation between Caenorhabditis elegans and human tyrosine hydroxylase, the key enzyme in the synthesis of dopamine.Semantic proximity Read ↗

RNAi of 14-3-3eta protein increases intracellular stability of tyrosine hydroxylase.Semantic proximity Read ↗

Brain catecholamine depletion and motor impairment in a Th knock-in mouse with type B tyrosine hydroxylase deficiency.Semantic proximity Read ↗

Influence of human tryptophan hydroxylase 2 N- and C-terminus on enzymatic activity and oligomerization.Semantic proximity Read ↗

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.Semantic proximity Read ↗

Multiple molecular determinants in the carboxyl terminus regulate dopamine transporter export from endoplasmic reticulum.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.