Identification of essential tryptophan in amylomaltase from Corynebacterium glutamicum

Rachadech, Wanitcha; Nimpiboon, Pitchanan; Naumthong, Wachiraporn; Nakapong, Santhana; Krusong, Kuakarun; Pongsawasdi, Piamsook

doi:10.1016/j.ijbiomac.2015.02.035

Cited by 16 publications

(11 citation statements)

References 29 publications

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“…The modification Biotech Health Sci. 2017; 4(1):e40191.caused significant decrease in enzyme activity, indicating that tryptophan residues are very important for catalysis (28). As shown in Figure 4B, the quenching data were analyzed using Stern-Volmer equation 1 and it was proven the static mode of interaction between NBS and MT.…”

Section: Discussionmentioning

confidence: 94%

Kinetic, Thermodynamic and Structural Studies of Native and N-Bromosuccinimide-Modified Mushroom Tyrosinase

Emami¹,

Gheibi

2016

Biotech Health Sci

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Background: Mushroom tyrosinase (MT) as a metalloenzyme is a good model for mechanistic studies of melanogenesis. To recognize the mechanism of MT action, it is important to investigate its inhibition, activation, mutation, and modification properties. Objectives: In this study, the chemical modification of MT tryptophan residues was carried out by using N-bromosuccinimide (NBS) and then, the activity, stability, and structure of the native and modified enzymes were compared. Methods: Chemical modification of MT tryptophan residues was accomplished by enzyme incubation with different concentrations of NBS. The relative activity of native and modified MT was investigated through catecholase enzyme reaction in presence of dihydroxyphenylalanine (L-Dopa) as substrate. Thermodynamic parameters including standard Gibbs free energy change (∆G25°C) and Melting temperature (Tm) were obtained from thermal denaturation of the native and modified enzymes. The circular dichroism and intrinsic fluorescence techniques were used to study secondary and tertiary structure of MT, respectively. All experiments were conducted in 2015 in biophysical laboratory of Qazvin University of Medical Sciences and Islamic Azad University, Science and Research Branch, Tehran. Results: The relative activity reduced from 100% for native enzyme to 10%, 7.9%, and 6.4% for modified MT with different NBS of

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Section: Discussionmentioning

confidence: 94%

Kinetic, Thermodynamic and Structural Studies of Native and N-Bromosuccinimide-Modified Mushroom Tyrosinase

Emami¹,

Gheibi

2016

Biotech Health Sci

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“…Amylomaltase from C. glutamicum ( Cg AM) is a biologically and industrially important enzyme. Cg AM was characterized, analyzed, engineered, and crystallized by Pongsawasdi et al for cyclodextrin production and starch modification, notwithstanding a report on the crystal structure of Cg AM. ,− Recently, a crystal structure of amylomaltase (MalQ) from mesophilic E. coli , which has an amino acid similarity of 30% to Cg AM, has been reported …”

Section: Introductionmentioning

confidence: 99%

Crystal Structure of Amylomaltase from Corynebacterium glutamicum

Joo

Kim

Seo

et al. 2016

J. Agric. Food Chem.

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Amylomaltase is an essential enzyme in maltose utilization and maltodextrin metabolism, and it has been industrially used for the production of cyclodextrin and modification of starch. We determined the crystal structure of amylomaltase from Corynebacterium glutamicum (CgAM) at a resolution of 1.7 Å. Although CgAM forms a dimer without NaCl, it exists as a monomer in physiological concentration of NaCl. CgAM is composed of N- and C-terminal domains, which can be further divided into two and four subdomains, respectively. It exhibits a unique structural feature at the functionally unknown N-domain and also shows two striking differences at the C-domain compared to other amylomaltases. These differences at extended edge of the substrate-binding site might affect substrate specificity for large cyclodextrin formation. The bis-tris methane and sulfate molecules bound at the substrate-binding site of our current structure mimic the binding of the hydroxyl groups of glucose bound at subsites -1 and -2, respectively.

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“…Among these enzymes, 4‐α‐glucanotransferases (4α‐Gtase, EC 2.4.1.25) from GH families 13, 57, and 77 catalyze the transfer from one α‐1,4‐glucan to another α‐1,4‐glucan or glucose with a free 4‐hydroxyl group, which have been received considerable attention recently due to the development of a number of new commercial products, such as cyclodextrin, maltodextrin, and functional oligosaccharides . Up to now, as the main types of 4‐α‐glucanotransferases, the disproportionating enzymes (D‐enzymes) from plants and amylomaltases (AMs) from microorganisms have been extensively investigated …”

Section: Introductionmentioning

confidence: 99%

“…The 4‐α‐glucanotransferases belonging to the GH77 family have been found to possess diverse enzymatic characteristics from the biochemical and structural analysis of the 25 characterized proteins (CAZY database). Members of the GH77 family have been identified in archaea, for example, the amylomaltase MalQ from Pyrobaculum aerophilum IM2, bacteria, for example, the MalQ from Escherichia coli MG1655 and CgAM from Corynebacterium glutamicum ATCC 13032 (BAB99690), as well as in eukaryotes such as the potato, barley, and Arabidopsis . These identified glucanotransferases are distinct from those that produce cyclic glucans with different DPs, such as the T. aquaticus amylomaltase which preferentially produced large cycloamyloses with DPs of more than 60, while D‐enzymes produced small cycloamyloses with DPs of less than 17 …”

Section: Introductionmentioning

confidence: 99%

Gene Expression and Biochemical Characterization of a GH77 4‐α‐Glucanotransferase CcGtase From Corallococcus sp. EGB

Zheng

Zhang

et al. 2019

Starch Stärke

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The enzyme 4‐α‐glucanotransferase catalyzes the intramolecular and intermolecular transglycosylation of α‐1,4‐glucan, which plays an important role in starch metabolism and starch modification. In this study, the gene encoding a 4‐α‐glucanotransferase from Corallococcus sp. EGB (ccGtase) is cloned and expressed in Escherichia coli BL21 (DE3). CcGtase contains all the conserved amino acid residues of glycoside hydrolase family 77 (GH77), which form the active site environment of the enzymes in the α‐amylase family, while sequence alignments show that 4‐α‐glucanotransferases from myxobacteria constitute an independent group along with the GH77 glucanotransferases. Product analysis shows that CcGtase is able to convert malto‐oligosaccharides and starch into linear maltooligosaccharides with a low degree of polymerization (DP < 12) instead of cycloamylose. The transfer action toward starch is only observed in the presence of glucose, and delayed production of maltose from the transfer reaction is also observed. During the reaction, no apparent hydrolytic activity is observed. Based on the low sequence identity (9–35%) and unique characteristics, CcGtase can be regarded as a new member of the GH77 family.

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Identification of essential tryptophan in amylomaltase from Corynebacterium glutamicum

Cited by 16 publications

References 29 publications

Kinetic, Thermodynamic and Structural Studies of Native and N-Bromosuccinimide-Modified Mushroom Tyrosinase

Kinetic, Thermodynamic and Structural Studies of Native and N-Bromosuccinimide-Modified Mushroom Tyrosinase

Crystal Structure of Amylomaltase from Corynebacterium glutamicum

Gene Expression and Biochemical Characterization of a GH77 4‐α‐Glucanotransferase CcGtase From Corallococcus sp. EGB

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