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Literature summary for 3.2.1.6 extracted from

  • Gaiser, O.J.; Piotukh, K.; Ponnuswamy, M.N.; Planas, A.; Borriss, R.; Heinemann, U.
    Structural basis for the substrate specificity of a Bacillus 1,3-1,4-beta-glucanase (2006), J. Mol. Biol., 357, 1211-1225.
    View publication on PubMed
Search for more literature for 3.2.1.6

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapor-diffusion at room temperature, space group P2(1)2(1)2(1), cell parameters: a = 75.77 A, b = 88.76 A, c = 154.79 A. High-resolution crystal structure of the hybrid 1,3-1,4-beta-glucanase H(A16-M)E105Q/E109Q in complex with a beta-glucan tetrasaccharide Paenibacillus macerans

Protein Variants

Protein Variants Comment Organism
A98W turnover-number for lichenan is 1.3fold lower than wild-type value, turnover-number for laminarin is 1.4fold higher than wild-type value Paenibacillus macerans
E131Q turnover-number for lichenan is 3.9fold lower than wild-type value, turnover-number for laminarin is 1.2fold lower than wild-type value Paenibacillus macerans
E63D turnover-number for lichenan is 10.5fold lower than wild-type value, turnover-number for laminarin is 27.1fold lower than wild-type value Paenibacillus macerans
E63Q turnover-number for lichenan is 147fold lower than wild-type value, turnover-number for laminarin is 67.4fold lower than wild-type value Paenibacillus macerans
H99D turnover-number for lichenan is 4.3fold lower than wild-type value, turnover-number for laminarin is 1.3fold lower than wild-type value Paenibacillus macerans
H99R turnover-number for lichenan is 8.1fold lower than wild-type value, turnover-number for laminarin is 1.5fold lowerthan wild-type value Paenibacillus macerans
N26A turnover-number for lichenan is 4.5fold lower than wild-type value, turnover-number for laminarin is 5.8fold lower than wild-type value Paenibacillus macerans
R65A turnover-number for lichenan is 1.5fold lower than wild-type value, turnover-number for laminarin is 2.8fold lower than wild-type value Paenibacillus macerans
S90A turnover-number for lichenan is 3.7fold lower than wild-type value, turnover-number for laminarin is 4.7fold lower than wild-type value Paenibacillus macerans
W184Y turnover-number for lichenan is 7.3fold lower than wild-type value, turnover-number for laminarin is 2.8fold lower than wild-type value Paenibacillus macerans
W192A turnover-number for lichenan is 29.4fold lower than wild-type value, turnover-number for laminarin is 12.5fold lower than wild-type value Paenibacillus macerans
Y123A turnover-number for lichenan is 29.5fold lower than wild-type value, turnover-number for laminarin is 12.5fold lower than wild-type value Paenibacillus macerans
Y123F turnover-number for lichenan is 1.9fold lower than wild-type value, turnover-number for laminarin is 2.5fold higher than wild-type value Paenibacillus macerans
Y24A turnover-number for lichenan is 3.7fold lower than wild-type value, turnover-number for laminarin is 3.8fold lower than wild-type value Paenibacillus macerans
Y24F turnover-number for lichenan is 2.5fold lower than wild-type value, turnover-number for laminarin is 1.5fold lower than wild-type value Paenibacillus macerans
Y24W turnover-number for lichenan is 1.5fold lower than wild-type value, turnover-number for laminarin is 1.9fold higher than wild-type value Paenibacillus macerans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Paenibacillus macerans

Organism

Organism UniProt Comment Textmining
Paenibacillus macerans
-
 H(A16-M), a 1,3-1,4-beta-glucanase from Bacillus macerans in which the 16 N-terminal residues have been replaced by the respective residues of the enzyme from Bacillus amyloliquefaciens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
laminarin + H2O
-
 Paenibacillus macerans ?
-
 ?
lichenan + H2O
-
 Paenibacillus macerans ?
-
 ?
additional information the ten active-site residues ASn26,Glu63, Arg65, Phe92, Tyr94, Glu105, Asp107, Glu109, Asn182 and Trp184 form a network of hydrogen bonds and hydrophobic stacking interactions with the substrate Paenibacillus macerans ?
-
 ?

Synonyms

Synonyms Comment Organism
H(A16-M) 1,3-1,4-beta-glucanase from Bacillus macerans in which the 16 N-terminal residues have been replaced by the respective residues of the enzyme from Bacillus amyloliquefaciens Paenibacillus macerans

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.047
-
 lichenan pH 7.2, 50°C, mutant enzyme E131Q Paenibacillus macerans
8.08
-
 lichenan pH 7.2, 50°C, mutant enzyme E63Q Paenibacillus macerans
27
-
 lichenan pH 7.2, 50°C, mutant enzyme E63D Paenibacillus macerans
40.4
-
 lichenan pH 7.2, 50°C, mutant enzyme Y123A Paenibacillus macerans
40.5
-
 lichenan pH 7.2, 50°C, mutant enzyme W192A Paenibacillus macerans
112.6
-
 lichenan pH 7.2, 50°C, mutant enzyme E63D Paenibacillus macerans
147.1
-
 lichenan pH 7.2, 50°C, mutant enzyme H99R Paenibacillus macerans
163.8
-
 lichenan pH 7.2, 50°C, mutant enzyme W184Y Paenibacillus macerans
262
-
 lichenan pH 7.2, 50°C, mutant enzyme N26A Paenibacillus macerans
276
-
 lichenan pH 7.2, 50°C, mutant enzyme H99D Paenibacillus macerans
302.4
-
 lichenan pH 7.2, 50°C, mutant enzyme E131Q Paenibacillus macerans
324
-
 lichenan pH 7.2, 50°C, mutant enzyme S90A Paenibacillus macerans
325
-
 lichenan pH 7.2, 50°C, mutant enzyme Y24A Paenibacillus macerans
481
-
 lichenan pH 7.2, 50°C, mutant enzyme Y24F Paenibacillus macerans
627
-
 lichenan pH 7.2, 50°C, mutant enzyme Y123F Paenibacillus macerans
787
-
 lichenan pH 7.2, 50°C, mutant enzyme Y24W Paenibacillus macerans
811
-
 lichenan pH 7.2, 50°C, mutant enzyme R65A Paenibacillus macerans
908
-
 lichenan pH 7.2, 50°C, mutant enzyme A98W Paenibacillus macerans
1191
-
 lichenan pH 7.2, 50°C, wild-type enzyme Paenibacillus macerans