beta-lactamase I from Bacillus cereus. Structure and site-directed mutagenesis.
about
Inactivation of the RTEM-1 cysteine beta-lactamase by iodoacetate. The nature of active-site functional groups and comparisons with the native enzymeBeta-lactamase of Bacillus licheniformis 749/C at 2 A resolutionFlexibility Correlation between Active Site Regions Is Conserved across Four AmpC β-Lactamase EnzymesBeta-lactamase TEM1 of E. coli. Crystal structure determination at 2.5 A resolutionThe importance of a critical protonation state and the fate of the catalytic steps in class A beta-lactamases and penicillin-binding proteins.Identification of residues critical for catalysis in a class C beta-lactamase by combinatorial scanning mutagenesis.Probing beta-lactamase structure and function using random replacement mutagenesis.Biochemical-genetic analysis and distribution of FAR-1, a class A beta-lactamase from Nocardia farcinicaChromosomal beta-lactamase genes of Klebsiella oxytoca are divided into two main groups, blaOXY-1 and blaOXY-2.Bovine intestinal bacteria inactivate and degrade ceftiofur and ceftriaxone with multiple beta-lactamases.Site-directed mutagenesis of beta-lactamase I: role of Glu-166.Role of the conserved amino acids of the 'SDN' loop (Ser130, Asp131 and Asn132) in a class A beta-lactamase studied by site-directed mutagenesis.Cloning, nucleotide sequence, and expression of the Bacillus cereus 5/B/6 beta-lactamase II structural gene.Extension of the substrate spectrum by an amino acid substitution at residue 219 in the Citrobacter freundii cephalosporinase.Effect of side-chain amide thionation on turnover of beta-lactam substrates by beta-lactamases. Further evidence on the question of side-chain hydrogen-bonding in catalysis.Beta-lactamases as fully efficient enzymes. Determination of all the rate constants in the acyl-enzyme mechanism.The diversity of the catalytic properties of class A beta-lactamases.Point mutations of two arginine residues in the Streptomyces R61 DD-peptidase.Kinetic characterization of the acyl-enzyme mechanism for beta-lactamase I.Kinetic and physical studies of beta-lactamase inhibition by a novel penem, BRL 42715.Site-directed mutagenesis of beta-lactamase I. Single and double mutants of Glu-166 and Lys-73.A standard numbering scheme for the class A beta-lactamases.Substitution of aspartic acid-217 of Citrobacter freundii cephalosporinase and properties of the mutant enzymes.A survey of a functional amino acid of class C beta-lactamase corresponding to Glu166 of class A beta-lactamases.Efficient production of secretory Streptomyces clavuligerus β-lactamase inhibitory protein (BLIP) in Pichia pastoris.
P2860
Q24529544-D1A60480-EB2B-476A-BF74-4422B9A35BB1Q27683632-1B0A3B02-8607-46BD-AA1C-96CAD3AB85F4Q28262501-1B26474E-718B-4FFC-BEFC-D05C831D7E1BQ28284595-32B7E010-6C00-4189-B6A0-4BB909EC4CBDQ30932666-D8065D1E-2E4A-4E8B-A2A9-732F7C963069Q30968138-7423758F-2467-4905-BD1D-EB6C496D0217Q31161561-60389D10-2100-442F-A757-763340D011B4Q33977117-DF700AC4-B201-42F6-9439-A45929CE9D4EQ35122518-0CF1EC92-363A-4C99-9BE7-E5690D095FBFQ35364206-96609074-0A9C-438E-840C-3978B649D8D3Q38308727-8BF58919-B838-44DF-81F2-EB782D497E6AQ38338744-5CB469B0-CF01-4D7B-A529-04E1B606FBD3Q39953559-1172BE2B-55D8-4B92-8B85-4F194F7D773DQ39960518-F4F8E263-00E0-499E-8F79-5876102468C9Q41783495-2CB89FD5-D537-4EB9-A0A1-43E96277D1F1Q41847833-DFA9D866-E9EE-442E-BF91-63CE523B0A5CQ41981406-BBE9ED01-9E9A-4E56-96C6-B97E2BBF255AQ42099606-722FE8C6-EEA1-4761-8CCE-6B7929429EFAQ42122541-67CF64AB-CB3E-4803-B9D6-249C7F8A0CBDQ42831248-204E2D79-C80B-48AE-8E60-D2D3A3B94BDCQ42859478-AB4BED39-7CCE-41BA-9E25-763EF30702B7Q42861944-37C5FE00-9601-4231-9251-5305CA679E7BQ54323934-93AF70C9-BD41-4B7E-AABB-637F6ADE9695Q54649856-2C6DD5AF-A7CF-42FE-9D1C-F138D606DB9EQ55322279-EACC4A7B-FD04-4FCB-BEDE-CC3E3735291C
P2860
beta-lactamase I from Bacillus cereus. Structure and site-directed mutagenesis.
description
1987 nî lūn-bûn
@nan
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
1987年论文
@zh
1987年论文
@zh-cn
name
beta-lactamase I from Bacillus cereus. Structure and site-directed mutagenesis.
@en
type
label
beta-lactamase I from Bacillus cereus. Structure and site-directed mutagenesis.
@en
prefLabel
beta-lactamase I from Bacillus cereus. Structure and site-directed mutagenesis.
@en
P2860
P356
P1433
P1476
beta-lactamase I from Bacillus cereus. Structure and site-directed mutagenesis.
@en
P2093
P2860
P304
P356
10.1042/BJ2480657
P407
P577
1987-12-01T00:00:00Z