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Results: 1-7 |
Results: 7
CRYSTALLOGRAPHIC COMPLEXES OF GLUCOAMYLASE WITH MALTOOLIGOSACCHARIDE ANALOGS - RELATIONSHIP OF STEREOCHEMICAL DISTORTIONS AT THE NONREDUCING END TO THE CATALYTIC MECHANISM
Authors: ALESHIN AE STOFFER B FIRSOV LM SVENSSON B HONZATKO RB
Citation: Ae. Aleshin et al., CRYSTALLOGRAPHIC COMPLEXES OF GLUCOAMYLASE WITH MALTOOLIGOSACCHARIDE ANALOGS - RELATIONSHIP OF STEREOCHEMICAL DISTORTIONS AT THE NONREDUCING END TO THE CATALYTIC MECHANISM, Biochemistry, 35(25), 1996, pp. 8319-8328
REFINED STRUCTURE FOR THE COMPLEX OF D-GLUCO-DIHYDROACARBOSE WITH GLUCOAMYLASE FROM ASPERGILLUS-AWAMORI VAR X100 TO 2.2-ANGSTROM RESOLUTION- DUAL CONFORMATIONS FOR EXTENDED INHIBITORS BOUND TO THE ACTIVE-SITEOF GLUCOAMYLASE
Authors: STOFFER B ALESHIN AE FIRSOV LM SVENSSON B HONZATKO RB
Citation: B. Stoffer et al., REFINED STRUCTURE FOR THE COMPLEX OF D-GLUCO-DIHYDROACARBOSE WITH GLUCOAMYLASE FROM ASPERGILLUS-AWAMORI VAR X100 TO 2.2-ANGSTROM RESOLUTION- DUAL CONFORMATIONS FOR EXTENDED INHIBITORS BOUND TO THE ACTIVE-SITEOF GLUCOAMYLASE, FEBS letters, 358(1), 1995, pp. 57-61
THERMODYNAMICS OF INHIBITOR BINDING TO MUTANT FORMS OF GLUCOAMYLASE FROM ASPERGILLUS-NIGER DETERMINED BY ISOTHERMAL TITRATION CALORIMETRY
Authors: BERLAND CR SIGURSKJOLD BW STOFFER B FRANDSEN TP SVENSSON B
Citation: Cr. Berland et al., THERMODYNAMICS OF INHIBITOR BINDING TO MUTANT FORMS OF GLUCOAMYLASE FROM ASPERGILLUS-NIGER DETERMINED BY ISOTHERMAL TITRATION CALORIMETRY, Biochemistry, 34(32), 1995, pp. 10153-10161
MUTATIONAL ANALYSIS OF THE ROLES IN CATALYSIS AND SUBSTRATE RECOGNITION OF ARGININE-54 AND ARGININE-305, ASPARTIC-ACID-309, AND TRYPTOPHAN-317 LOCATED AT SUBSITE-1 AND SUBSITE-2 IN GLUCOAMYLASE FROM ASPERGILLUS-NIGER
Authors: FRANDSEN TP CHRISTENSEN T STOFFER B LEHMBECK J DUPONT C HONZATKO RB SVENSSON B
Citation: Tp. Frandsen et al., MUTATIONAL ANALYSIS OF THE ROLES IN CATALYSIS AND SUBSTRATE RECOGNITION OF ARGININE-54 AND ARGININE-305, ASPARTIC-ACID-309, AND TRYPTOPHAN-317 LOCATED AT SUBSITE-1 AND SUBSITE-2 IN GLUCOAMYLASE FROM ASPERGILLUS-NIGER, Biochemistry, 34(32), 1995, pp. 10162-10169
NMR-SPECTROSCOPY OF EXCHANGEABLE PROTONS OF GLUCOAMYLASE AND OF COMPLEXES WITH INHIBITORS IN THE 9-15-PPM RANGE
Authors: FIRSOV LM NEUSTROEV KN ALESHIN AE METZLER CM METZLER DE SCOTT RD STOFFER B CHRISTENSEN T SVENSSON B
Citation: Lm. Firsov et al., NMR-SPECTROSCOPY OF EXCHANGEABLE PROTONS OF GLUCOAMYLASE AND OF COMPLEXES WITH INHIBITORS IN THE 9-15-PPM RANGE, European journal of biochemistry, 223(1), 1994, pp. 293-302
SITE-DIRECTED MUTAGENESIS OF THE CATALYTIC BASE GLUTAMIC-ACID-400 IN GLUCOAMYLASE FROM ASPERGILLUS-NIGER AND OF TYROSINE-48 AND GLUTAMINE-401, BOTH HYDROGEN-BONDED TO THE GAMMA-CARBOXYLATE GROUP OF GLUTAMIC-ACID-400
Authors: FRANDSEN TP DUPONT C LEHMBECK J STOFFER B SIERKS MR HONZATKO RB SVENSSON B
Citation: Tp. Frandsen et al., SITE-DIRECTED MUTAGENESIS OF THE CATALYTIC BASE GLUTAMIC-ACID-400 IN GLUCOAMYLASE FROM ASPERGILLUS-NIGER AND OF TYROSINE-48 AND GLUTAMINE-401, BOTH HYDROGEN-BONDED TO THE GAMMA-CARBOXYLATE GROUP OF GLUTAMIC-ACID-400, Biochemistry, 33(46), 1994, pp. 13808-13816
PRODUCTION, PURIFICATION AND CHARACTERIZATION OF THE CATALYTIC DOMAINOF GLUCOAMYLASE FROM ASPERGILLUS-NIGER
Authors: STOFFER B FRANDSEN TP BUSK PK SCHNEIDER P SVENDSEN I SVENSSON B
Citation: B. Stoffer et al., PRODUCTION, PURIFICATION AND CHARACTERIZATION OF THE CATALYTIC DOMAINOF GLUCOAMYLASE FROM ASPERGILLUS-NIGER, Biochemical journal, 292, 1993, pp. 197-202
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