Site-directed mutagenesis study of the three catalytic residues of the fructosyltransferases of Lactobacillus reuteri 121.
about
Structure-function relationships of glucansucrase and fructansucrase enzymes from lactic acid bacteriaImpaired coordination of nucleophile and increased hydrophobicity in the +1 subsite shift levansucrase activity towards transfructosylation.Donor substrate recognition in the raffinose-bound E342A mutant of fructosyltransferase Bacillus subtilis levansucraseStructural insights into glycoside hydrolase family 32 and 68 enzymes: functional implications.Unraveling the difference between invertases and fructan exohydrolases: a single amino acid (Asp-239) substitution transforms Arabidopsis cell wall invertase1 into a fructan 1-exohydrolase.Mutational analysis of the active center of plant fructosyltransferases: Festuca 1-SST and barley 6-SFT.The role of conserved inulosucrase residues in the reaction and product specificity of Lactobacillus reuteri inulosucrase.The probiotic Lactobacillus johnsonii NCC 533 produces high-molecular-mass inulin from sucrose by using an inulosucrase enzyme.Draft Genome Sequence of Lactobacillus reuteri 121, a Source of α-Glucan and β-Fructan Exopolysaccharides.A Bacillus megaterium plasmid system for the production, export, and one-step purification of affinity-tagged heterologous levansucrase from growth medium.Mutational analysis of the role of calcium ions in the Lactobacillus reuteri strain 121 fructosyltransferase (levansucrase and inulosucrase) enzymes.Mutational analysis of conserved regions harboring catalytic triad residues of the levansucrase protein encoded by the lsc-3 gene (lsc3) of Pseudomonas syringae pv. tomato DC3000.
P2860
Q24544122-F0117738-E990-40A4-858A-BC134C61EF2AQ30491874-69A3FBF9-E6DE-414E-AEA6-CE446D76C0CEQ33325643-473EBDC6-8F6E-46F0-8EF9-E0D7D73AB735Q37364315-56A5C036-A0E8-4DEC-9C74-F57960C22349Q38298252-CCB3A8A8-2E1E-4D5A-9C06-3E3C27F68C7AQ38322224-D2EC75A9-3282-4040-ABB8-765E060262B5Q38323298-27BC0550-7D37-4270-AE90-2C2F372688F8Q39022726-B227807D-105D-4169-B324-957B63F58DCAQ41834395-521F9536-DF61-48B3-A9BA-8AA39333215AQ43234608-274365A7-C9A3-4AB4-8F7E-9845B63253FBQ45264596-209A6A40-1E24-4722-8CAC-B84E0F402012Q46888010-6E9A7563-8D36-4416-BF89-2384F0D90D0B
P2860
Site-directed mutagenesis study of the three catalytic residues of the fructosyltransferases of Lactobacillus reuteri 121.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh-hant
name
Site-directed mutagenesis stud ...... of Lactobacillus reuteri 121.
@en
Site-directed mutagenesis stud ...... of Lactobacillus reuteri 121.
@nl
type
label
Site-directed mutagenesis stud ...... of Lactobacillus reuteri 121.
@en
Site-directed mutagenesis stud ...... of Lactobacillus reuteri 121.
@nl
prefLabel
Site-directed mutagenesis stud ...... of Lactobacillus reuteri 121.
@en
Site-directed mutagenesis stud ...... of Lactobacillus reuteri 121.
@nl
P2093
P2860
P1433
P1476
Site-directed mutagenesis stud ...... of Lactobacillus reuteri 121.
@en
P2093
Dijkhuizen L
van Der Maarel MJ
van Geel-Schutten GH
van Hijum SA
van Koningsveld GA
P2860
P304
P356
10.1016/S0014-5793(04)00085-7
P407
P577
2004-02-01T00:00:00Z