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

The three-dimensional structural basis of type II hyperprolinemia.

Journal of molecular biology - 13 Jul 2012

Srivastava Dhiraj, Singh Ranjan K, Moxley Michael A, Henzl Michael T, Becker Donald F, Tanner John J

Abstract excerpt

Type II hyperprolinemia is an autosomal recessive disorder caused by a deficiency in Δ(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH; also known as ALDH4A1), the aldehyde dehydrogenase that catalyzes the oxidation of glutamate semialdehyde to glutamate. Here, we report the first structure of hu...

Read the complete abstract on PubMed

Topics

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

Share to Alanine
Share to Amino Acid Metabolism, Inborn Errors
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrogen Bonding

Share to Leucine

Share to Protein Folding

Share to Serine

Source

Open in PubMed Open full text

Identifiers

PMID: 22516612
DOI: 10.1016/j.jmb.2012.04.010
PMCID: PMC3372638

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-22516612-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The three-dimensional structural basis of type II hyperprolinemia.PMID 22516612Read ↗

Insights into Aldehyde Dehydrogenase Enzymes: A Structural PerspectiveSemantic proximity Read ↗

Structural and biochemical studies of human 4-hydroxy-2-oxoglutarate aldolase: implications for hydroxyproline metabolism in primary hyperoxaluria.Semantic proximity Read ↗

Computational approach to unravel the impact of missense mutations of proteins (D2HGDH and IDH2) causing D-2-hydroxyglutaric aciduria 2.Semantic proximity Read ↗

Structure of the Mitochondrial Aminolevulinic Acid Synthase, a Key Heme Biosynthetic Enzyme.Semantic proximity Read ↗

Mutations in the Delta1-pyrroline 5-carboxylate dehydrogenase gene cause type II hyperprolinemia.Semantic proximity Read ↗

Structural basis of the dysfunctioning of human 2-oxo acid dehydrogenase complexes.Semantic proximity Read ↗

Solvent accessibility of E1α and E1β residues with known missense mutations causing pyruvate dehydrogenase complex (PDC) deficiency: Impact on PDC-E1 structure and function.Semantic proximity Read ↗

In Silico Analysis of the L-2-Hydroxyglutarate Dehydrogenase Gene Mutations and Their Biological Impact on Disease Etiology.Semantic proximity Read ↗

Structural basis of substrate specificity in human glyoxylate reductase/hydroxypyruvate reductase.Semantic proximity Read ↗

Crystal structure and interaction studies of human DHTKD1 provide insight into a mitochondrial megacomplex in lysine catabolismSemantic proximity Read ↗

Structural insight of dopamine β-hydroxylase, a drug target for complex traits, and functional significance of exonic single nucleotide polymorphisms.Semantic proximity Read ↗

Gamma glutamyl semialdehyde dehydrogenase: simulations on native and mutant forms support the importance of outer shell lysines.Semantic proximity Read ↗

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