Substrate specificity and molecular cloning of the lily endo-beta-mannosidase acting on N-glycan.

Substrate specificity and molecular cloning of the lily endo-beta-mannosidase acting on N-glycan. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Substrate specificity and molecular cloning of the lily endo-beta-mannosidase acting on N-glycan. Abstract Text:

Akiko Sasaki,Takeshi Ishimizu,Sumihiro Hase,

Endo-beta-mannosidase, which hydrolyzes the Manbeta1-4GlcNAc linkage in the trimannosyl core structure of N-glycans, was recently purified to homogeneity from lily (Lilium longiflorum) flowers as a heterotrimer [Ishimizu, T., Sasaki, A., Okutani, S., Maeda, M., Yamagishi, M., and Hase, S. (2004) J. Biol. Chem. 279, 38555-38562]. Here, we describe the substrate specificity of the enzyme and cloning of its cDNA. The purified enzyme hydrolyzed pyridylaminated (PA-) Man(n)Manalpha1-6Manbeta1-4GlcNAcbeta1-4GlcNAc (n = 0-2) to Man(n)Manalpha1-6Man and GlcNAcbeta1-4GlcNAc-PA. It did not hydrolyze PA-sugar chains containing Manalpha1-3Manbeta and/or Xylbeta1-2Manbeta. The best substrate among the PA-sugar chains tested was Manalpha1-6Manbeta1-4GlcNAcbeta1-4GlcNAc-PA with a K(m) value of 1.2 mM. However, the enzyme displayed a marked preference for the corresponding glycopeptide, Manalpha1-6Manbeta1-4GlcNAcbeta1-4GlcNAc-peptide (K(m) value 75 microM). These results indicate that the substrate recognition by the enzyme involves the peptide portion attached to the N-glycan. Sequence information on the purified enzyme was used to clone the corresponding cDNA. The monocotyledonous lily enzyme (952 amino acids) displays 68% identity to its dicotyledonous (Arabidopsis thaliana) homologue. Our results show that the heterotrimeric enzyme is encoded by a single gene that gives rise to three polypeptides following posttranslational proteolysis. The enzyme is ubiquitously expressed, suggesting that it has a general function such as processing or degrading N-glycans.

Substrate specificity and molecular cloning of the lily endo-beta-mannosidase acting on N-glycan. Publishing Authors By Initials

A Sasaki,T Ishimizu,S Hase,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research

PUBMED ID PMID:

MEDLINE DATE:

Substrate specificity and molecular cloning of the lily endo-beta-mannosidase acting on N-glycan. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 137

Page Numbers: 87-93

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jan

YEAR: 2005

Substrate specificity and molecular cloning of the lily endo-beta-mannosidase acting on N-glycan. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Substrate specificity and molecular cloning of the lily endo-beta-mannosidase acting on N-glycan. Keywords Mesh Terms:

KEYWORDS: Substrate Specificity

MESH TERMS: genetics

Chemical & Substance for Abstract: Substrate specificity and molecular cloning of the lily endo-beta-mannosidase acting on N-glycan. Information

Substance Name: endo-beta-mannosidase

Registry Number: EC 3.2.1.-

Grant and Affiliation Information for Substrate specificity and molecular cloning of the lily endo-beta-mannosidase acting on N-glycan.

AFFILIATION: Department of Chemistry, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan.

Country: Japan

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER: AB185918

Number Hits: 0

Substrate specificity and molecular cloning of the lily endo-beta-mannosidase acting on N-glycan Related Publications

• A new disaccharide Fuc alpha 1-2Man found in human urine.
• A new hydrolase specific for taurine-conjugates of bile acids.
• A new method of determination of hydroxamic acid by its urease inhibition and application to biochemical studies.
• Characterization of carbohydrate-binding specificity of concanavalin A by competitive binding of pyridylamino sugar chains.
• Co(II)-regulated substrate specificity of cytosolic alpha-mannosidase.
• Conversion of pyridylamino sugar chains to 1-amino-1-deoxy derivatives, intermediates for tagging with fluorescein and biotin.
• Conversion of pyridylamino sugar chains to corresponding reducing sugar chains.
• Detection of human urinary alpha-amylase encoded by the AMY2B gene using a fluorogenic substrate, FG5P.
• Determination of lectin-sugar binding constants by microequilibrium dialysis coupled with high performance liquid chromatography.
• Free oligosaccharides with Lewis x structure expressed in the segmentation period of zebrafish embryo.
• History of acute coronary events during the predialysis phase of chronic kidney disease is a strong risk factor for major adverse cardiac events in patients initiating haemodialysis.
• In vitro stabilization and minimum active component of polygalacturonic acid synthase involved in pectin biosynthesis.
• Inhibition of urease activity by hydroxamic acid derivatives of amino acids.
• Linkage position analysis of pyridylamino-disaccharides by HPLC of fluorogenic Smith degradation products.
• Photo-oxidation of Jack bean urease in the presence of methylene blue.
• Processing pathway deduced from the structures of N-glycans in Carica papaya.
• Purification and characterization of hen oviduct alpha 1,2-mannosidase.
• Purification and substrate specificity of UDP-D-xylose:beta-D-glucoside alpha-1,3-D-xylosyltransferase involved in the biosynthesis of the Xyl alpha1-3Xyl alpha1-3Glc beta1-O-Ser on epidermal growth factor-like domains.
• Quantitation and isomeric structure analysis of free oligosaccharides present in the cytosol fraction of mouse liver: detection of a free disialobiantennary oligosaccharide and glucosylated oligomannosides.
• Release of O-linked sugar chains from glycoproteins with anhydrous hydrazine and pyridylamination of the sugar chains with improved reaction conditions.
• Representing and selecting vibrational angular momentum states for quasiclassical trajectory chemical dynamics simulations.
• Structural analysis of N-linked sugar chains of human blood clotting factor IX.
• Structural analysis of O-linked sugar chains in human blood clotting factor IX.
• Structural analysis of the sugar chains of human urinary thrombomodulin.
• Structures of N-linked sugar chains expressed mainly in mouse brain.
• Studies on the substrate specificity of neutral alpha-mannosidase purified from Japanese quail oviduct by using sugar chains from glycoproteins.
• Substrate specificity of bovine liver cytosolic neutral alpha-mannosidase activated by Co2+.
• Theoretical study of the molecular structure and normal coordinate analysis of hydrogen cyanide addition compound with boron trifluoride, HCN-BF(3).
• [Silent myocardial ischemia]
• beta1-4Galactosyltransferase activity of mouse brain as revealed by analysis of brain-specific complex-type N-linked sugar chains.