the petm11 vector Search Results


bacterial expression vector petm11 embl  (New England Biolabs)
99
New England Biolabs bacterial expression vector petm11 embl
Bacterial Expression Vector Petm11 Embl, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/the+petm11+vector/pm34895045-87-16-28?v=New+England+Biolabs
Average 99 stars, based on 1 article reviews
bacterial expression vector petm11 embl - by Bioz Stars, 2026-08
99/100 stars
  Buy from Supplier
petm11 vector  (Addgene inc)
93
Addgene inc petm11 vector
Petm11 Vector, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/the+petm11+vector/khanal_satyam__2022__chemoenzymatic_generation_of_lipid_membranes-526-61-70?v=Addgene+inc
Average 93 stars, based on 1 article reviews
petm11 vector - by Bioz Stars, 2026-08
93/100 stars
  Buy from Supplier
petm 11 vector  (Addgene inc)
96
Addgene inc petm 11 vector
Petm 11 Vector, supplied by Addgene inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/the+petm11+vector/pmc09108631-167-1-11?v=Addgene+inc
Average 96 stars, based on 1 article reviews
petm 11 vector - by Bioz Stars, 2026-08
96/100 stars
  Buy from Supplier
rs iha  (GenScript corporation)
90
GenScript corporation rs iha
( a ) Overall structure of the La <t>IHA</t> dimer found in the asymmetric unit, the protomers are colored green and cyan and shown in two different orientations rotated by 90 degrees. Manganese and highlighted residues a location of active sites in the dimer. ( b ) Isatinate and benzyl benzoate in the substrate binding pocket of La IHA. Isatinate is coordinating bidentate directly to the manganese. Parts of the pocket, residues Trp61 and Trp59, are contributed by the opposing monomer via the hairpin swap. Key binding pocket residues of the La IHB binding pocket (grey) are functionally conserved. ( c ) Catalytically important residue in the active site of La IHA: benzyl benzoate. The corresponding site of La IHA: benzyl benzoate is superposed (transparent). The manganese is found in octahedral coordination similarly to that described in . Gln219 resides in a double conformation and only partially coordinates to the manganese. Also, W1025 is found in a double conformation (denoted A and B in Fig. 1). Note that Asp75 is coordinating bidentate in La IHA:isatinate while monodentate in La IHA: benzyl benzoate. ( d ) The isatin hydrolysis by La IHA (circles) and <t>Rs</t> <t>IHA</t> (triangles) follows Michaelis-Menten kinetics, and the parameters are collected in f). ( e ) Both La IHA and Rs IHA display strong manganese dependency. ( f ) Kinetic parameters of La IHA and Rs IHA collected with previous values from La IHB and activated mutant La IHB S225C. All measurements in ( d ) and ( e ) were performed in triplets.
Rs Iha, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/the+petm11+vector/pmc06117287-42-1-8?v=GenScript+corporation
Average 90 stars, based on 1 article reviews
rs iha - by Bioz Stars, 2026-08
90/100 stars
  Buy from Supplier
xhoi  (New England Biolabs)
99
New England Biolabs xhoi
( a ) Overall structure of the La <t>IHA</t> dimer found in the asymmetric unit, the protomers are colored green and cyan and shown in two different orientations rotated by 90 degrees. Manganese and highlighted residues a location of active sites in the dimer. ( b ) Isatinate and benzyl benzoate in the substrate binding pocket of La IHA. Isatinate is coordinating bidentate directly to the manganese. Parts of the pocket, residues Trp61 and Trp59, are contributed by the opposing monomer via the hairpin swap. Key binding pocket residues of the La IHB binding pocket (grey) are functionally conserved. ( c ) Catalytically important residue in the active site of La IHA: benzyl benzoate. The corresponding site of La IHA: benzyl benzoate is superposed (transparent). The manganese is found in octahedral coordination similarly to that described in . Gln219 resides in a double conformation and only partially coordinates to the manganese. Also, W1025 is found in a double conformation (denoted A and B in Fig. 1). Note that Asp75 is coordinating bidentate in La IHA:isatinate while monodentate in La IHA: benzyl benzoate. ( d ) The isatin hydrolysis by La IHA (circles) and <t>Rs</t> <t>IHA</t> (triangles) follows Michaelis-Menten kinetics, and the parameters are collected in f). ( e ) Both La IHA and Rs IHA display strong manganese dependency. ( f ) Kinetic parameters of La IHA and Rs IHA collected with previous values from La IHB and activated mutant La IHB S225C. All measurements in ( d ) and ( e ) were performed in triplets.
Xhoi, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/the+petm11+vector/custom%40r0146%4010%2E1107%2Fs2053230x14016458?v=New+England+Biolabs
Average 99 stars, based on 1 article reviews
xhoi - by Bioz Stars, 2026-08
99/100 stars
  Buy from Supplier
ncoi  (New England Biolabs)
97
New England Biolabs ncoi
( a ) Overall structure of the La <t>IHA</t> dimer found in the asymmetric unit, the protomers are colored green and cyan and shown in two different orientations rotated by 90 degrees. Manganese and highlighted residues a location of active sites in the dimer. ( b ) Isatinate and benzyl benzoate in the substrate binding pocket of La IHA. Isatinate is coordinating bidentate directly to the manganese. Parts of the pocket, residues Trp61 and Trp59, are contributed by the opposing monomer via the hairpin swap. Key binding pocket residues of the La IHB binding pocket (grey) are functionally conserved. ( c ) Catalytically important residue in the active site of La IHA: benzyl benzoate. The corresponding site of La IHA: benzyl benzoate is superposed (transparent). The manganese is found in octahedral coordination similarly to that described in . Gln219 resides in a double conformation and only partially coordinates to the manganese. Also, W1025 is found in a double conformation (denoted A and B in Fig. 1). Note that Asp75 is coordinating bidentate in La IHA:isatinate while monodentate in La IHA: benzyl benzoate. ( d ) The isatin hydrolysis by La IHA (circles) and <t>Rs</t> <t>IHA</t> (triangles) follows Michaelis-Menten kinetics, and the parameters are collected in f). ( e ) Both La IHA and Rs IHA display strong manganese dependency. ( f ) Kinetic parameters of La IHA and Rs IHA collected with previous values from La IHB and activated mutant La IHB S225C. All measurements in ( d ) and ( e ) were performed in triplets.
Ncoi, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/the+petm11+vector/custom%40r0193%4010%2E1107%2Fs2053230x14016458?v=New+England+Biolabs
Average 97 stars, based on 1 article reviews
ncoi - by Bioz Stars, 2026-08
97/100 stars
  Buy from Supplier
petm11  (Helmholtz Zentrum fur Infektionsforschung GmbH)
90
Helmholtz Zentrum fur Infektionsforschung GmbH petm11
( a ) Overall structure of the La <t>IHA</t> dimer found in the asymmetric unit, the protomers are colored green and cyan and shown in two different orientations rotated by 90 degrees. Manganese and highlighted residues a location of active sites in the dimer. ( b ) Isatinate and benzyl benzoate in the substrate binding pocket of La IHA. Isatinate is coordinating bidentate directly to the manganese. Parts of the pocket, residues Trp61 and Trp59, are contributed by the opposing monomer via the hairpin swap. Key binding pocket residues of the La IHB binding pocket (grey) are functionally conserved. ( c ) Catalytically important residue in the active site of La IHA: benzyl benzoate. The corresponding site of La IHA: benzyl benzoate is superposed (transparent). The manganese is found in octahedral coordination similarly to that described in . Gln219 resides in a double conformation and only partially coordinates to the manganese. Also, W1025 is found in a double conformation (denoted A and B in Fig. 1). Note that Asp75 is coordinating bidentate in La IHA:isatinate while monodentate in La IHA: benzyl benzoate. ( d ) The isatin hydrolysis by La IHA (circles) and <t>Rs</t> <t>IHA</t> (triangles) follows Michaelis-Menten kinetics, and the parameters are collected in f). ( e ) Both La IHA and Rs IHA display strong manganese dependency. ( f ) Kinetic parameters of La IHA and Rs IHA collected with previous values from La IHB and activated mutant La IHB S225C. All measurements in ( d ) and ( e ) were performed in triplets.
Petm11, supplied by Helmholtz Zentrum fur Infektionsforschung GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/the+petm11+vector/pmc05603727-231-6-23?v=Helmholtz+Zentrum+fur+Infektionsforschung+GmbH
Average 90 stars, based on 1 article reviews
petm11 - by Bioz Stars, 2026-08
90/100 stars
  Buy from Supplier
pgem-t  (Promega)
90
Promega pgem-t
( a ) Overall structure of the La <t>IHA</t> dimer found in the asymmetric unit, the protomers are colored green and cyan and shown in two different orientations rotated by 90 degrees. Manganese and highlighted residues a location of active sites in the dimer. ( b ) Isatinate and benzyl benzoate in the substrate binding pocket of La IHA. Isatinate is coordinating bidentate directly to the manganese. Parts of the pocket, residues Trp61 and Trp59, are contributed by the opposing monomer via the hairpin swap. Key binding pocket residues of the La IHB binding pocket (grey) are functionally conserved. ( c ) Catalytically important residue in the active site of La IHA: benzyl benzoate. The corresponding site of La IHA: benzyl benzoate is superposed (transparent). The manganese is found in octahedral coordination similarly to that described in . Gln219 resides in a double conformation and only partially coordinates to the manganese. Also, W1025 is found in a double conformation (denoted A and B in Fig. 1). Note that Asp75 is coordinating bidentate in La IHA:isatinate while monodentate in La IHA: benzyl benzoate. ( d ) The isatin hydrolysis by La IHA (circles) and <t>Rs</t> <t>IHA</t> (triangles) follows Michaelis-Menten kinetics, and the parameters are collected in f). ( e ) Both La IHA and Rs IHA display strong manganese dependency. ( f ) Kinetic parameters of La IHA and Rs IHA collected with previous values from La IHB and activated mutant La IHB S225C. All measurements in ( d ) and ( e ) were performed in triplets.
Pgem T, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/the+petm11+vector/pmc05283164-57-18-19?v=Promega
Average 90 stars, based on 1 article reviews
pgem-t - by Bioz Stars, 2026-08
90/100 stars
  Buy from Supplier
petm11 vector  (New England Biolabs)
99
New England Biolabs petm11 vector
( a ) Overall structure of the La <t>IHA</t> dimer found in the asymmetric unit, the protomers are colored green and cyan and shown in two different orientations rotated by 90 degrees. Manganese and highlighted residues a location of active sites in the dimer. ( b ) Isatinate and benzyl benzoate in the substrate binding pocket of La IHA. Isatinate is coordinating bidentate directly to the manganese. Parts of the pocket, residues Trp61 and Trp59, are contributed by the opposing monomer via the hairpin swap. Key binding pocket residues of the La IHB binding pocket (grey) are functionally conserved. ( c ) Catalytically important residue in the active site of La IHA: benzyl benzoate. The corresponding site of La IHA: benzyl benzoate is superposed (transparent). The manganese is found in octahedral coordination similarly to that described in . Gln219 resides in a double conformation and only partially coordinates to the manganese. Also, W1025 is found in a double conformation (denoted A and B in Fig. 1). Note that Asp75 is coordinating bidentate in La IHA:isatinate while monodentate in La IHA: benzyl benzoate. ( d ) The isatin hydrolysis by La IHA (circles) and <t>Rs</t> <t>IHA</t> (triangles) follows Michaelis-Menten kinetics, and the parameters are collected in f). ( e ) Both La IHA and Rs IHA display strong manganese dependency. ( f ) Kinetic parameters of La IHA and Rs IHA collected with previous values from La IHB and activated mutant La IHB S225C. All measurements in ( d ) and ( e ) were performed in triplets.
Petm11 Vector, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/the+petm11+vector/10__1074_slash_jbc__m609974200-57-13-17?v=New+England+Biolabs
Average 99 stars, based on 1 article reviews
petm11 vector - by Bioz Stars, 2026-08
99/100 stars
  Buy from Supplier
mbptrap hp column  (Cytiva Europe)
95
Cytiva Europe mbptrap hp column
( a ) Overall structure of the La <t>IHA</t> dimer found in the asymmetric unit, the protomers are colored green and cyan and shown in two different orientations rotated by 90 degrees. Manganese and highlighted residues a location of active sites in the dimer. ( b ) Isatinate and benzyl benzoate in the substrate binding pocket of La IHA. Isatinate is coordinating bidentate directly to the manganese. Parts of the pocket, residues Trp61 and Trp59, are contributed by the opposing monomer via the hairpin swap. Key binding pocket residues of the La IHB binding pocket (grey) are functionally conserved. ( c ) Catalytically important residue in the active site of La IHA: benzyl benzoate. The corresponding site of La IHA: benzyl benzoate is superposed (transparent). The manganese is found in octahedral coordination similarly to that described in . Gln219 resides in a double conformation and only partially coordinates to the manganese. Also, W1025 is found in a double conformation (denoted A and B in Fig. 1). Note that Asp75 is coordinating bidentate in La IHA:isatinate while monodentate in La IHA: benzyl benzoate. ( d ) The isatin hydrolysis by La IHA (circles) and <t>Rs</t> <t>IHA</t> (triangles) follows Michaelis-Menten kinetics, and the parameters are collected in f). ( e ) Both La IHA and Rs IHA display strong manganese dependency. ( f ) Kinetic parameters of La IHA and Rs IHA collected with previous values from La IHB and activated mutant La IHB S225C. All measurements in ( d ) and ( e ) were performed in triplets.
Mbptrap Hp Column, supplied by Cytiva Europe, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/the+petm11+vector/custom%4028918778%4028950029?v=Cytiva+Europe
Average 95 stars, based on 1 article reviews
mbptrap hp column - by Bioz Stars, 2026-08
95/100 stars
  Buy from Supplier

Image Search Results


( a ) Overall structure of the La IHA dimer found in the asymmetric unit, the protomers are colored green and cyan and shown in two different orientations rotated by 90 degrees. Manganese and highlighted residues a location of active sites in the dimer. ( b ) Isatinate and benzyl benzoate in the substrate binding pocket of La IHA. Isatinate is coordinating bidentate directly to the manganese. Parts of the pocket, residues Trp61 and Trp59, are contributed by the opposing monomer via the hairpin swap. Key binding pocket residues of the La IHB binding pocket (grey) are functionally conserved. ( c ) Catalytically important residue in the active site of La IHA: benzyl benzoate. The corresponding site of La IHA: benzyl benzoate is superposed (transparent). The manganese is found in octahedral coordination similarly to that described in . Gln219 resides in a double conformation and only partially coordinates to the manganese. Also, W1025 is found in a double conformation (denoted A and B in Fig. 1). Note that Asp75 is coordinating bidentate in La IHA:isatinate while monodentate in La IHA: benzyl benzoate. ( d ) The isatin hydrolysis by La IHA (circles) and Rs IHA (triangles) follows Michaelis-Menten kinetics, and the parameters are collected in f). ( e ) Both La IHA and Rs IHA display strong manganese dependency. ( f ) Kinetic parameters of La IHA and Rs IHA collected with previous values from La IHB and activated mutant La IHB S225C. All measurements in ( d ) and ( e ) were performed in triplets.

Journal: Scientific Reports

Article Title: A fundamental catalytic difference between zinc and manganese dependent enzymes revealed in a bacterial isatin hydrolase

doi: 10.1038/s41598-018-31259-y

Figure Lengend Snippet: ( a ) Overall structure of the La IHA dimer found in the asymmetric unit, the protomers are colored green and cyan and shown in two different orientations rotated by 90 degrees. Manganese and highlighted residues a location of active sites in the dimer. ( b ) Isatinate and benzyl benzoate in the substrate binding pocket of La IHA. Isatinate is coordinating bidentate directly to the manganese. Parts of the pocket, residues Trp61 and Trp59, are contributed by the opposing monomer via the hairpin swap. Key binding pocket residues of the La IHB binding pocket (grey) are functionally conserved. ( c ) Catalytically important residue in the active site of La IHA: benzyl benzoate. The corresponding site of La IHA: benzyl benzoate is superposed (transparent). The manganese is found in octahedral coordination similarly to that described in . Gln219 resides in a double conformation and only partially coordinates to the manganese. Also, W1025 is found in a double conformation (denoted A and B in Fig. 1). Note that Asp75 is coordinating bidentate in La IHA:isatinate while monodentate in La IHA: benzyl benzoate. ( d ) The isatin hydrolysis by La IHA (circles) and Rs IHA (triangles) follows Michaelis-Menten kinetics, and the parameters are collected in f). ( e ) Both La IHA and Rs IHA display strong manganese dependency. ( f ) Kinetic parameters of La IHA and Rs IHA collected with previous values from La IHB and activated mutant La IHB S225C. All measurements in ( d ) and ( e ) were performed in triplets.

Article Snippet: The Rs IHA (UniProtKB: Q8XYC3) was ordered from Genscript and inserted into the expression vector pET-M11.

Techniques: Binding Assay, Residue, Mutagenesis