WordNet

an enzyme that catalyses the biochemical reduction of some specified substance

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1. ビリルビン代謝 bilirubin metabolism
2. 新生児における非抱合型高ビリルビン血症の発症機序および病因 pathogenesis and etiology of unconjugated hyperbilirubinemia in the newborn
3. 成人における溶血性貧血の診断へのアプローチ approach to the diagnosis of hemolytic anemia in the adult
4. 黄疸または無症候性高ビリルビン血症の分類および原因 classification and causes of jaundice or asymptomatic hyperbilirubinemia
5. 急性間欠性ポルフィリン症のマネージメントおよび予後 management and prognosis of acute intermittent porphyria

English Journal

Two Structures of a Thiazolinyl Imine Reductase from Yersinia enterocolitica (Irp3) Provide Insight for Catalysis and Binding to the Nonribosomal Peptide Synthetase Module of HMWP1.

Meneely KM, Lamb AL.AbstractThe thiazolinyl imine reductase from Yersinia enterocolitica (Irp3) catalyzes the NADPH-dependent reduction of the thiazoline ring in an intermediate for the formation of the siderophore yersiniabactin. Two structures of Irp3 were determined in the apo- (1.85 Å) and NADP(+)-bound (2.31 Å) forms. Irp3 shows structural homology to sugar oxidoreductases such as glucose-fructose oxidoreductase and 1,5-anhydro-D-fructose reductase, as well as to biliverdin reductase. A homology model of the thiazolinyl imine reductase from Pseudomonas aeruginosa (PchG) was generated. Extensive loop insertions are observed in the C-terminal domain that are unique to Irp3 and PchG and not found in the structural homologs that recognize small molecular substrates. These loops are hypothesized to be important for binding of the nonribosomal peptide synthetase modules (found in HMWP1 and PchF, respectively) to which the substrate of the reductase is covalently attached. A catalytic mechanism of proton donation from a general acid (either histidine-101 or tyrosine-128) and hydride donation from C4 of nicotinamide of the NADPH cofactor is proposed for reduction of the carbon-nitrogen double bond of the thiazoline.
Biochemistry.Biochemistry.2012 Oct 15. [Epub ahead of print]
The thiazolinyl imine reductase from Yersinia enterocolitica (Irp3) catalyzes the NADPH-dependent reduction of the thiazoline ring in an intermediate for the formation of the siderophore yersiniabactin. Two structures of Irp3 were determined in the apo- (1.85 Å) and NADP(+)-bound (2.31 Å) forms.
PMID 23066849

Molecular modeling to provide insight into the substrate binding and catalytic mechanism of human biliverdin-IXα reductase.

Fu G, Liu H, Doerksen RJ.SourceDepartment of Medicinal Chemistry, School of Pharmacy, University of Mississippi, University, Mississippi 38677, United States.
The journal of physical chemistry. B.J Phys Chem B.2012 Aug 16;116(32):9580-94. doi: 10.1021/jp301456j. Epub 2012 Aug 7.
Human biliverdin-IXα reductase (hBVR-A) catalyzes the conversion of biliverdin-IXα to bilirubin-IXα in the last step of heme degradation and is a key enzyme in regulating a wide range of cellular responses. Though the X-ray structure of hBVR-A is available including cofactor, a crystal structure
PMID 22823425