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

Mutational study on alphaGln90 of Fe-type nitrile hydratase from Rhodococcus sp. N771.

Bioscience, biotechnology, and biochemistry - 1 Apr 2006

Takarada Hiromi, Kawano Yoshiaki, Hashimoto Kouichi, Nakayama Hiroshi, Ueda Shunsaku, Yohda Masafumi, Kamiya Nobuo, Dohmae Naoshi, Maeda Mizuo, Odaka Masafumi

Abstract excerpt

Nitrile hydratase (NHase) from Rhodococcus sp. N771 is a non-heme iron enzyme having post-translationally modified cysteine ligands, alphaCys112-SO2H and alphaCys114-SOH. We replaced alphaGln90, which is conserved in all known NHases and involved in the hydrogen-bond network around the catalytic...

Read the complete abstract on PubMed

Topics

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

Share to Cysteine
Share to Glutamine
Share to Hydro-Lyases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrogen Bonding

Share to Nitriles

Share to Rhodococcus

Share to Spectrum Analysis

Source

Identifiers

PMID: 16636455
DOI: 10.1271/bbb.70.881

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-16636455-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutational study on alphaGln90 of Fe-type nitrile hydratase from Rhodococcus sp. N771.PMID 16636455Read ↗

Kinetic and structural studies on roles of the serine ligand and a strictly conserved tyrosine residue in nitrile hydratase.Semantic proximity Read ↗

Analyzing the catalytic role of active site residues in the Fe-type nitrile hydratase from Comamonas testosteroni Ni1.Semantic proximity Read ↗

Mutational and structural analysis of cobalt-containing nitrile hydratase on substrate and metal binding.Semantic proximity Read ↗

X-ray crystal structure of a mutant assimilatory nitrite reductase that shows sulfite reductase-like activity.Semantic proximity Read ↗

Alpha Carbonic Anhydrase from Nitratiruptor tergarcus Engineered for Increased Activity and Thermostability.Semantic proximity Read ↗

Proposal for a hydrogen bond network in the active site of the prototypic gamma-class carbonic anhydrase.Semantic proximity Read ↗

Crystal structure of an enzyme-substrate complex provides insight into the interaction between human arylsulfatase A and its substrates during catalysis.Semantic proximity Read ↗

Unexpected NADPH Hydratase Activity in the Nitrile Reductase QueF from Escherichia coli.Semantic proximity Read ↗

Kinetics and computational studies of ligand migration in nitrophorin 7 and its Δ1-3 mutant.Semantic proximity Read ↗

Insertion of an H-bonding residue into the distal pocket of the ferriheme protein nitrophorin 4: effect on nitrite-iron coordination and nitrite disproportionation.Semantic proximity Read ↗

Catalytic roles for two water bridged residues (Asp-98 and His-255) in the active site of copper-containing nitrite reductase.Semantic proximity Read ↗

Structural insights into the conformational change of Staphylococcus aureus NreA at C-terminus.Semantic proximity Read ↗

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