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

Role of Tyr201 and Tyr385 in substrate activation by p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens.

European journal of biochemistry - 15 Aug 1993

Eschrich K, van der Bolt F J, de Kok A, van Berkel W J

Abstract excerpt

The crystal structure of the enzyme-substrate complex of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens shows that the hydroxyl group of 4-hydroxybenzoate interacts with the side chain of Tyr201, which is in close contact with the side chain of Tyr385. The role of this hydrogen bonding network in substrate activation was studied by kinetic and spectral analysis of Tyr-->Phe mutant enzymes. The...

Read the complete abstract on PubMed

Topics

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

Share to Base Sequence
Share to Binding Sites
Share to Enzyme Activation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli

Share to Hydrogen-Ion Concentration

Share to Kinetics

Share to Molecular Sequence Data

Share to Mutation

Source

Identifiers

PMID: 8365400
DOI: 10.1111/j.1432-1033.1993.tb18125.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

Role of Tyr201 and Tyr385 in substrate activation by p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens.PMID 8365400Read ↗

Crystal structures of wild-type p-hydroxybenzoate hydroxylase complexed with 4-aminobenzoate,2,4-dihydroxybenzoate, and 2-hydroxy-4-aminobenzoate and of the Tyr222Ala mutant complexed with 2-hydroxy-4-aminobenzoate. Evidence for a proton channel and a new binding mode of the flavin ring.Semantic proximity Read ↗

Lys42 and Ser42 variants of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens reveal that Arg42 is essential for NADPH binding.Semantic proximity Read ↗

Crystal structures of mutant Pseudomonas aeruginosa p-hydroxybenzoate hydroxylases: the Tyr201Phe, Tyr385Phe, and Asn300Asp variants.Semantic proximity Read ↗

Mechanistic insights into p-hydroxybenzoate hydroxylase from studies of the mutant Ser212Ala.Semantic proximity Read ↗

Considerations on activity determinants of fungal polyphenol oxidases based on mutational and structural studiesSemantic proximity Read ↗

Structure and function of mutant Arg44Lys of 4-hydroxybenzoate hydroxylase implications for NADPH binding.Semantic proximity Read ↗

Protein dynamics and electrostatics in the function of p-hydroxybenzoate hydroxylase.Semantic proximity Read ↗

Spectroscopy and kinetics of wild-type and mutant tyrosine hydroxylase: mechanistic insight into O2 activation.Semantic proximity Read ↗

Conserved tyrosine-369 in the active site of Escherichia coli copper amine oxidase is not essential.Semantic proximity Read ↗

Properties of p-hydroxybenzoate hydroxylase when stabilized in its open conformation.Semantic proximity Read ↗

The role of the conserved residues His-246, His-199, and Tyr-255 in the catalysis of catechol 2,3-dioxygenase from Pseudomonas stutzeri OX1.Semantic proximity Read ↗

Enhancement of L-tryptophan 5-hydroxylation activity by structure-based modification of L-phenylalanine 4-hydroxylase from Chromobacterium violaceum.Semantic proximity Read ↗

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