Chitinase from<i>Autographa californica</i>Multiple Nucleopolyhedrovirus: Rapid Purification from Sf-9 Medium and Mode of Action

Fukamizo, Tamo; Sato, Hírokazu; Mizuhara, Mamiko; Ohnuma, Takayuki; Gotoh, Tetsuo; Hiwatashi, Koichi; Takahashi, Saori

doi:10.1271/bbb.110300

Cited by 8 publications

(6 citation statements)

References 30 publications

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“…Although GH18 chitinases are widely distributed in living organisms from bacteria to humans [2][3][4][5][6], GH19 enzymes are only found in plants and some bacteria [7]. Plants constitutively or inducibly produce various types of GH18 and GH19 chitinases [8].…”

Section: Introductionmentioning

confidence: 99%

“…Chitinases (EC 3.2.1.14) hydrolyze β‐1,4‐glycosidic linkages of chitin, and have been classified into families GH18 and GH19 according to the CAZy database (http://www.cazy.org/) [1]. Although GH18 chitinases are widely distributed in living organisms from bacteria to humans [2–6], GH19 enzymes are only found in plants and some bacteria [7]. Plants constitutively or inducibly produce various types of GH18 and GH19 chitinases [8].…”

Section: Introductionmentioning

confidence: 99%

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Complete subsite mapping of a “loopful” GH19 chitinase from rye seeds based on its crystal structure

et al. 2013

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Edited by Richard Cogdell Keywords:Crystal structure GH19 chitinase Rye seed Chitin oligosaccharide Domain motion a b s t r a c t Crystallographic analysis of a mutated form of ''loopful'' GH19 chitinase from rye seeds a double mutant RSC-c, in which Glu67 and Trp72 are mutated to glutamine and alanine, respectively, (RSC-c-E67Q/W72A) in complex with chitin tetrasaccharide (GlcNAc) 4 revealed that the entire substrate-binding cleft was completely occupied with the sugar residues of two (GlcNAc) 4 molecules. One (GlcNAc) 4 molecule bound to subsites À4 to À1, while the other bound to subsites +1 to +4. Comparisons of the main chain conformation between liganded RSC-c-E67Q/W72A and unliganded wild type RSC-c suggested domain motion essential for catalysis. This is the first report on the complete subsite mapping of GH19 chitinase.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Complete subsite mapping of a “loopful” GH19 chitinase from rye seeds based on its crystal structure

et al. 2013

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“…TG by family GH 18 chitinases from viruses to humans is known. Chitinase from Autographa californica multiple nucleopolyhedrovirus produced TG products DP6 and DP8 from 4.6 to 5.0 mM DP4 to DP6 substrates (10). Chitotriosidase from human macrophages synthesized the TG products up to DP6 to DP9 from 5 mM DP5 substrate (1).…”

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confidence: 99%

Synthesis of Long-Chain Chitooligosaccharides by a Hypertransglycosylating Processive Endochitinase of Serratia proteamaculans 568

Purushotham

Podile

2012

J Bacteriol

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We describe the heterologous expression and characterization of a 407-residue single-domain glycosyl hydrolase family 18 chitinase (SpChiD) from Gram-negative Serratia proteamaculans 568 that has unprecedented catalytic properties. SpChiD was optimally active at pH 6.0 and 40°C, where it showed a K m of 83 mg ml ؊1 , a k cat of 3.9 ؋ 10 2 h ؊1 , and a k cat /K m of 4.7 h mg ؊1 ml ؊1 on colloidal chitin. On chitobiose, the K m , k cat , and k cat /K m were 203 M, 1.3 ؋ 10 2 h ؊1 , and 0.62 h ؊1 M ؊1 , respectively. Hydrolytic activity on chitooligosaccharides (CHOS) and colloidal chitin indicated that SpChiD was an endo-acting processive enzyme, with the unique ability to convert released chitobiose to N-acetylglucosamine, the major end product. SpChiD showed hyper transglycosylation (TG) with trimer-hexamer CHOS substrates, generating considerable amounts of long-chain CHOS. The TG activity of SpChiD was dependent on both the length and concentration of the oligomeric substrate and also on the enzyme concentration. The length and amount of accumulated TG products increased with increases in the length of the substrate and its concentration and decreased with increases in the enzyme concentration. The SpChiD bound to insoluble and soluble chitin substrates despite the absence of accessory domains. Sequence alignments and structural modeling indicated that SpChiD would have a deep substrate-binding groove lined with aromatic residues, which is characteristic of processive enzymes. SpChiD shows a combination of properties that seems rare among family 18 chitinases and that may resemble the properties of human chitotriosidase.

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“…First report of a glycosynthase that employs amino sugar fluoride as a donor substrate (Ohnuma, et al, 2012) C1 α-LArabinohydrolases The cellulose-binding domain shown to be a thermostabilizing domain (Fukamizo et al, 2011) Chitinase Bacillus cereus TKU027 TOF (DHB) Purification and function (Wang et al, 2012f) Chitinase A Serratia marcescens TOF Study of substrate positioning Chitinase A1 Bacillus circulans TOF (DHB)…”

Section: Arabidopsis Thalianamentioning

confidence: 99%

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2011–2012

Harvey

2015

Mass Spectrometry Reviews

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This review is the seventh update of the original article published in 1999 on the application of MALDI mass spectrometry to the analysis of carbohydrates and glycoconjugates and brings coverage of the literature to the end of 2012. General aspects such as theory of the MALDI process, matrices, derivatization, MALDI imaging, and fragmentation are covered in the first part of the review and applications to various structural types constitute the remainder. The main groups of compound are oligo- and poly-saccharides, glycoproteins, glycolipids, glycosides, and biopharmaceuticals. Much of this material is presented in tabular form. Also discussed are medical and industrial applications of the technique, studies of enzyme reactions, and applications to chemical synthesis. © 2015 Wiley Periodicals, Inc. Mass Spec Rev 36:255-422, 2017.

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Chitinase fromAutographa californicaMultiple Nucleopolyhedrovirus: Rapid Purification from Sf-9 Medium and Mode of Action

Cited by 8 publications

References 30 publications

Complete subsite mapping of a “loopful” GH19 chitinase from rye seeds based on its crystal structure

Complete subsite mapping of a “loopful” GH19 chitinase from rye seeds based on its crystal structure

Synthesis of Long-Chain Chitooligosaccharides by a Hypertransglycosylating Processive Endochitinase of Serratia proteamaculans 568

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2011–2012

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