Novel enzyme activities and functional plasticity revealed by recombining highly homologous enzymes.
about
Diversification of catalytic function in a synthetic family of chimeric cytochrome p450sAncient Evolution and Recent Evolution Converge for the Biodegradation of Cyanuric Acid and Related TriazinesMicrobial enzymes: tools for biotechnological processesSolution structure of termicin, an antimicrobial peptide from the termite Pseudacanthotermes spinigerSynthetic shuffling expands functional protein diversity by allowing amino acids to recombine independently.Enhanced crossover SCRATCHY: construction and high-throughput screening of a combinatorial library containing multiple non-homologous crossovers.Revealing biases inherent in recombination protocols.Directed enzyme evolution via small and effective neutral drift libraries.Enzymatic degradation of chlorodiamino-s-triazine.Catalytic improvement and evolution of atrazine chlorohydrolase.The structure of the hexameric atrazine chlorohydrolase AtzAIntramolecular epistasis and the evolution of a new enzymatic functionEvolution of catabolic pathways: Genomic insights into microbial s-triazine metabolism.X-ray structure of the amidase domain of AtzF, the allophanate hydrolase from the cyanuric acid-mineralizing multienzyme complex.Modifying the stereochemistry of an enzyme-catalyzed reaction by directed evolution.Use of the University of Minnesota Biocatalysis/Biodegradation Database for study of microbial degradation.The enzymatic basis for pesticide bioremediation.From protein engineering to immobilization: promising strategies for the upgrade of industrial enzymesEffects of recombination on complex regulatory circuitsRecombinant organisms for production of industrial products.Toward protein engineering for phytoremediation: possibilities and challenges.Biocatalysts: application and engineering for industrial purposes.Diversity of nitrile hydratase and amidase enzyme genes in Rhodococcus erythropolis recovered from geographically distinct habitats.TrzN from Arthrobacter aurescens TC1 Is a zinc amidohydrolaseSubstrate specificity and colorimetric assay for recombinant TrzN derived from Arthrobacter aurescens TC1.Ongoing functional evolution of the bacterial atrazine chlorohydrolase AtzA.Survey of protein engineering strategiesHighly active enzymes by automated combinatorial backbone assembly and sequence design
P2860
Q24681772-7B063F89-90CB-4454-9D30-4970440109C5Q26771222-03CBFDC2-53DF-47C9-9F17-20F4F67FD1EAQ26827731-B628F4D1-F65E-4333-9F87-54E7612D233DQ27640519-295BC3D3-817D-4FE9-A05D-E54163ED6CB7Q30869909-5BCDD037-E92D-4FA4-B735-47A618D6B47CQ31016777-7EEED75C-AEC8-46EA-9683-2DCC5789AE4BQ33305483-226C7DB8-CA58-45FE-872E-9FBDD2BF4A53Q33377922-2F495E97-400F-4ED7-9019-D6D921CA19E6Q33961088-32767FFE-88BF-4FDC-B2C3-AF46F587AD7BQ34016021-04F4CDD4-0FBB-4CB3-9073-EA3EC7D36B1AQ34043420-BD5303ED-2C55-4F4A-8250-2F19D2D363C1Q34328302-A924183A-2040-4BE4-98E1-888AE10A01E1Q34572653-CE7D7576-0E5F-4A1C-BCB7-0DB5AC1AA6EEQ34777599-5393322C-BFAD-4878-8316-A48C3EF8B95DQ34867008-F896EED8-C80D-45B7-B5C1-81414D855CB2Q35958113-08330886-45FA-4531-A7D0-66E8DF2FC145Q36256240-28C9AC7D-9DCD-41FB-B5AF-99FE5D21203DQ36590032-5B71FE56-838F-4A06-B39B-DDDD884609EDQ37397493-29484936-B762-4B8B-8230-CB1AC17EFF20Q37843625-50F65E75-7778-4AC3-B75A-74C4A4A6B7ADQ37951977-E82E8656-8BDB-4570-A46F-865F06B3163BQ38265408-63AF9636-DD56-4A12-B16C-EB01C734EAA3Q39913477-54E3F0DA-145C-4EA1-8776-05BF71DE3B84Q42259720-20495175-DD10-41FF-A395-E4D4483FD4ADQ42727463-BE621251-A73C-4569-AD20-CB1667E1B08EQ46538353-AC46B95D-538B-48BD-99B4-105E98907A97Q56895981-6A48929D-9DF4-4458-8378-EC5C2DED7E12Q58061090-859CD060-AB41-46AE-A225-E9238626AA5B
P2860
Novel enzyme activities and functional plasticity revealed by recombining highly homologous enzymes.
description
2001 nî lūn-bûn
@nan
2001 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Novel enzyme activities and fu ...... ing highly homologous enzymes.
@ast
Novel enzyme activities and fu ...... ing highly homologous enzymes.
@en
type
label
Novel enzyme activities and fu ...... ing highly homologous enzymes.
@ast
Novel enzyme activities and fu ...... ing highly homologous enzymes.
@en
prefLabel
Novel enzyme activities and fu ...... ing highly homologous enzymes.
@ast
Novel enzyme activities and fu ...... ing highly homologous enzymes.
@en
P2093
P1476
Novel enzyme activities and fu ...... ing highly homologous enzymes.
@en
P2093
Bermudez E
Minshull J
Raillard S
Seffernick J
Stemmer WP
P304
P356
10.1016/S1074-5521(01)00061-8
P577
2001-09-01T00:00:00Z