Aromatic residues in the catalytic center of chitinase A from Serratia marcescens affect processivity, enzyme activity, and biomass converting efficiency.
about
Crystal Structures of Bacillus cereus NCTU2 Chitinase Complexes with Chitooligomers Reveal Novel Substrate Binding for Catalysis: A CHITINASE WITHOUT CHITIN BINDING AND INSERTION DOMAINSCrystal structure and mode of action of a class V chitinase from Nicotiana tabacumHallmarks of Processivity in Glycoside Hydrolases from Crystallographic and Computational Studies of the Serratia marcescens ChitinasesCrystal structure and chitin oligosaccharide-binding mode of a 'loopful' family GH19 chitinase from rye, Secale cereale, seedsStructure of a complete four-domain chitinase from Moritella marina, a marine psychrophilic bacteriumCel48A from Thermobifida fusca: structure and site directed mutagenesis of key residuesCarbohydrate binding module recognition of xyloglucan defined by polar contacts with branching xyloses and CH-Π interactionsNew insights into the enzymatic mechanism of human chitotriosidase (CHIT1) catalytic domain by atomic resolution X-ray diffraction and hybrid QM/MMActive site and laminarin binding in glycoside hydrolase family 55Multiple functions of aromatic-carbohydrate interactions in a processive cellulase examined with molecular simulationStructure, dynamics, and specificity of endoglucanase D from Clostridium cellulovoransCellulase processivity.Chitinase from Autographa californica multiple nucleopolyhedrovirus: rapid purification from Sf-9 medium and mode of action.Catalytic efficiency of chitinase-D on insoluble chitinous substrates was improved by fusing auxiliary domains.Synthesis of long-chain chitooligosaccharides by a hypertransglycosylating processive endochitinase of Serratia proteamaculans 568.Production of chitooligosaccharides and their potential applications in medicineBiotechnological approaches to develop bacterial chitinases as a bioshield against fungal diseases of plants.Transglycosylation by a chitinase from Enterobacter cloacae subsp. cloacae generates longer chitin oligosaccharidesCharacterization of two novel bacterial type A exo-chitobiose hydrolases having C-terminal 5/12-type carbohydrate-binding modules.The predominant molecular state of bound enzyme determines the strength and type of product inhibition in the hydrolysis of recalcitrant polysaccharides by processive enzymesKinetics of cellobiohydrolase (Cel7A) variants with lowered substrate affinity.Analysis of productive binding modes in the human chitotriosidase.Fungal chitinases: function, regulation, and potential roles in plant/pathogen interactions.The tryptophan residue at the active site tunnel entrance of Trichoderma reesei cellobiohydrolase Cel7A is important for initiation of degradation of crystalline cellulose.Processivity of cellobiohydrolases is limited by the substrate.Biochemical and mutational analyses of a multidomain cellulase/mannanase from Caldicellulosiruptor bescii.Structure, Catalysis, and Inhibition of OfChi-h, the Lepidoptera-exclusive Insect Chitinase.Slow Off-rates and Strong Product Binding Are Required for Processivity and Efficient Degradation of Recalcitrant Chitin by Family 18 ChitinasesStructural prediction of a novel chitinase from the psychrophilic Glaciozyma antarctica PI12 and an analysis of its structural properties and function.Characterization of a cold-adapted and salt-tolerant exo-chitinase (ChiC) from Pseudoalteromonas sp. DL-6.Inter-domain Synergism Is Required for Efficient Feeding of Cellulose Chain into Active Site of Cellobiohydrolase Cel7A.Loop variants of the thermophile Rasamsonia emersonii Cel7A with improved activity against cellulose.A small lytic polysaccharide monooxygenase from Streptomyces griseus targeting α- and β-chitin.Alanine substitution in cellobiohydrolase provides new insights into substrate threading.Systems analysis of the family Glycoside Hydrolase family 18 enzymes from Cellvibrio japonicus characterizes essential chitin degradation functions.Role of Tyr-435 of Vibrio harveyi chitinase A in chitin utilization.Two-way traffic of glycoside hydrolase family 18 processive chitinases on crystalline chitin.Cellulose chain binding free energy drives the processive move of cellulases on the cellulose surface.Chitinase: diversity, limitations, and trends in engineering for suitable applications
P2860
Q27663876-26497618-6F74-4A0D-B261-DA10DB451106Q27666525-09FA1883-308E-485B-AD82-B07B20E60D64Q27672373-84A550C6-70E1-4440-BCE6-46783001FFAFQ27681850-4F3A65A2-2C50-4F68-8681-9810ED8B26FBQ27684527-04B1FCCF-8518-4405-8542-E7B211BE7F73Q27687638-5B59712A-0076-4D04-BFB0-DD47C9D227CBQ27695696-ECBCE612-C5E9-47ED-8BE7-D7EFBBBFD621Q27701462-D9665218-D78D-4F73-985D-9BFB38AA958DQ30383966-92167775-A493-4D1E-ACE0-B3C8FB9B6BC9Q30407674-2D02670F-425E-4181-9BA7-D2C3CE8D455DQ33690592-5E960982-154D-47BE-BFDA-753A9A26DD21Q33860961-F76F462F-5674-46D8-B1E4-825FEB38F5FBQ34012546-1F2DA0E6-ED05-47E2-A6F9-E9FBCC833D00Q35548002-0D58E429-82FD-4F39-B6EF-587EB027733CQ36155308-7A918EEA-98F6-4F4C-8887-1D58D0FB406AQ37766095-DDF99A7A-BF54-475F-AD81-0B497F7FB97DQ37767245-11D4BFD4-1531-42F8-B435-9EFD6EBFA674Q38287761-1A2DF23B-5887-494A-AFAB-C3B4584CBC2AQ38288756-97431214-0A5F-42D8-876B-DF4CDA54F254Q38300474-A2DF9A06-0E7A-41EA-AC0B-6BBA8B6CDC8AQ38303808-6F75A4E1-53E3-4D6C-8C51-5F43E00F4D09Q38312582-0FF7940A-03E8-44EF-8A82-51A9AA0A4847Q38622999-7F36250B-C10A-4C62-805A-1D9237D84BDEQ40600573-9AB0835C-3215-4838-B2DA-4F253187F054Q41556498-82332634-3CF1-444C-9CED-0351AF007F59Q41783626-A7113EB4-62B5-4446-A844-C44D4C3852F4Q41988376-482BAF97-A3BA-459F-B6BB-8EC22FF4605CQ42155247-1127F485-3100-4DB8-8A3A-04FD6F30CE9CQ43015827-6CC11ABF-96F2-40D0-A9D7-180F787C5FAFQ43026609-82859AEC-3402-4350-91A2-0A796643DC24Q46356776-C20197E5-108F-4646-863E-BBBF5DDBD192Q46687534-DCF5FCDE-A4DF-4BE3-BC8B-CD37E409CAE1Q46784323-12E52EF5-98D0-423A-AFE8-66FB0DE513A6Q47130054-E6F66805-B44F-4AD5-AF39-1F15745976D7Q49789099-A9DB200F-9131-4944-91AA-34A7CF47CD3CQ50150732-8D264FDE-54BB-4030-A917-FD3BA174EBB8Q53534385-34F7B344-097B-4043-BA71-5E054510CD9FQ54250028-1CC27665-C19A-42C5-B602-FEBED93A50B5Q58693524-DAEE3D74-95D2-40B1-B285-F33BC999C14F
P2860
Aromatic residues in the catalytic center of chitinase A from Serratia marcescens affect processivity, enzyme activity, and biomass converting efficiency.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
Aromatic residues in the catal ...... biomass converting efficiency.
@en
type
label
Aromatic residues in the catal ...... biomass converting efficiency.
@en
prefLabel
Aromatic residues in the catal ...... biomass converting efficiency.
@en
P2093
P2860
P50
P356
P1476
Aromatic residues in the catal ...... biomass converting efficiency.
@en
P2093
Berit Bjugan Aam
Henrik Zakariassen
Kjell M Vårum
P2860
P304
10610-10617
P356
10.1074/JBC.M900092200
P407
P577
2009-02-25T00:00:00Z