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x * 97000, recombinant wild-type enzyme, SDS-PAGE, x * 66000, recombinant truncation mutant enzyme, SDS-PAGE
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x * 97000, recombinant wild-type enzyme, SDS-PAGE, x * 66000, recombinant truncation mutant enzyme, SDS-PAGE
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x * 91650, calculated from sequence
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x * 91650, calculated from sequence
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?
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x * 53527, isoform ASCHI53, x * 61202, isoform ASCHI61, MALDI-TOF. x * 4300, isoform ASCHI53, x * 55000, isoform ASCHI61, SDS-PAGE
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x * 89000, SDS-PAGE, isoenzyme 3
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x * 104000, SDS-PAGE, isoenzyme 7
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x * 112000, SDS-PAGE, isoenzyme 1
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x * 120000, SDS-PAGE, isoenzyme 6
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x * 117000, SDS-PAGE, isoenzymes 4, 5 and 8
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x * 115000, SDS-PAGE, isoenzyme 2
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x * 89000, SDS-PAGE, isoenzyme 3
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?
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x * 104000, SDS-PAGE, isoenzyme 7
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?
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x * 112000, SDS-PAGE, isoenzyme 1
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?
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x * 120000, SDS-PAGE, isoenzyme 6
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?
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x * 117000, SDS-PAGE, isoenzymes 4, 5 and 8
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?
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x * 45000, SDS-PAGE
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?
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x * 70000, SDS-PAGE
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?
x * 27800, SDS-PAGE, x * 27757, mature enzyme, sequence calculation
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x * 46000, SDS-PAGE
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?
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x * 36236, ESIMS analysis
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x * 74500, calculated, x * 69600, SDS-PAGE of recombinant enzyme
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x * 36000, SDS-PAGE
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?
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x * 36236, ESIMS analysis
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?
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x * 40000, SDS-PAGE
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?
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x * 72000, Chi72, SDS-PAGE
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x * 62000, SDS-PAGE, x * 62135, calculated
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x * 66801, calculated, x * 66000, SDS-PAGE
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x * 66801, calculated, x * 66000, SDS-PAGE
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?
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x * 72000, Chi72, SDS-PAGE
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?
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x * 41000, SDS-PAGE
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?
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x * 808000, SDS-PAGE
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?
x * 65878, mass spectrometry, x * 62500, recombinant His6-tagged SCChi-1, SDS-PAGE
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x * 85000, Chi1, SDS-PAGE, x * 30000, Chi2, SDS-PAGE, x * 55000, Chi3, SDS-PAGE
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x * 85000, Chi1, SDS-PAGE, x * 30000, Chi2, SDS-PAGE, x * 55000, Chi3, SDS-PAGE
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?
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x * 70665, calculated from nucleotide sequence
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x * 74500, calculated from seuence
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x * 74000, calculated
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x * 70000, mature enzyme lacking its signal peptide sequence, SDS-PAGE
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x * 74000, calculated
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x * 35700, glycosylated Chi3, SDS-PAGE, x * 28300, nonglycosylated Chi3, SDS-PAGE
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x * 65000, SDS-PAGE, isoenzyme 1, x * 88000, SDS-PAGE, isoenzyme 2
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x * 34000, SDS-PAGE
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?
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x * 26200, calculated from sequence
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x * 26534, major chitinase, mass spectrometry
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x * 26733, minor chitinase, mass spectrometry
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x * 61000, SDS-PAGE
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x * 54400, recombinant enzyme, SDS-PAGE
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x * 74400, recombinant enzyme, SDS-PAGE
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x * 80800, recombinant enzyme, SDS-PAGE
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x * 80800, recombinant enzyme, SDS-PAGE
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?
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x * 74400, recombinant enzyme, SDS-PAGE
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x * 54400, recombinant enzyme, SDS-PAGE
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?
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x * 24500, isozymes ChiA and ChiC, SDS-PAGE, x * 25500, isozyme ChiB, SDS-PAGE
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x * 32000, basic chitinase, SDS-PAGE
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x * 28000, acidic chitinase, SDS-PAGE
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x * 64000, SDS-PAGE
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?
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x * 28000, isoenzyme 1, SDS-PAGE, x * 25500, isoenzyme 2, SDS-PAGE, x * 23000, isoenzyme 3, SDS-PAGE, x * 24200, isoenzyme 4, SDS-PAGE, x * 24700, isoenzyme 5, SDS-PAGE, x * 25000, isoenzyme 6, SDS-PAGE, x * 25000, isoenzyme 7, SDS-PAGE
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x * 44000, recombinant His-tagged enzyme, SDS-PAGE
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x * 74651, calculated from sequence
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x * 74651, calculated from sequence
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?
x * 68000, recombinant enzyme
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x * 38000, SDS-PAGE of mature protein
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x * 30000, SDS-PAGE, EP3-1, x * 29000, SDS-PAGE, EP3-3, x * 34000, SDS-PAGE, DcChitI, x * 29000, SDS-PAGE, DcChitII
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x * 33500, SDS-PAGE, isoenzymes I-III
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x * 32000, recombinant deglycosylated enzyme, SDS-PAGE
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x * 31900, calculated from amino acid sequence
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x * 50000, recombinant enzyme fused to thioredoxin, SDS-PAGE
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x * 79000, recombinant His-tagged ChiB, SDS-PAGE, x * 120000, recombinant His-tagged ChiA, SDS-PAGE, x * 97000, about, recombinant His-tagged ChiA, sequence calculation
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x * 57800, SDS-PAGE, GAC2, x * 48200, SDS-PAGE, GAC1
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x * 25000, SDS-PAGE, x * 22654, mature enzyme, sequence calculation
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x * 30000, SDS-PAGE, GBC-a and GBC-b
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x * 66500, SDS-PAGE
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?
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x * 47000, isoenzyme HoChiC, SDS-PAGE
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x * 51000, isoenzyme HoChiB, SDS-PAGE
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x * 62000, isoenzyme HoChiA, SDS-PAGE
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x * 39000, SDS-PAGE, x * 50000, SDS-PAGE
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x * 39000-43000, SI-CLP, SDS-PAGE
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x * 60000, recombinant enzyme, SDS-PAGE, x * 59330, sequence calculation
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x * 60000, recombinant enzyme, SDS-PAGE, x * 59330, sequence calculation
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x * 31700, calculated, x * 31000, SDS-PAGE
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x * 38000, isoform Chi35, SDS-PAGE
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x * 82000, isoform Chi78, SDS-PAGE
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x * 82000, isoform Chi78, SDS-PAGE
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?
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x * 38000, isoform Chi35, SDS-PAGE
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?
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x * 85000, isoenzyme II, SDS-PAGE
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x * 64000, isoform Chi-64, SDS-PAGE
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x * 81000, SDS-PAGE
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?
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x * 78000, recombinant GST-tagged AMCase, SDS-PAGE
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x * 78000, recombinant GST-tagged AMCase, SDS-PAGE
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?
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x * 29000, recombinant soluble NaCHIT1, SDS-PAGE
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x * 66000, calculated from sequence
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Niallia circulans No. 4.1
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x * 66000, calculated from sequence
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x * 29900, calculated from sequence
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x * 31500, recombinant enzyme, SDS-PAGE
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x * 31500, recombinant enzyme, SDS-PAGE
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x * 33000, recombinant enzyme
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x * 33000, recombinant enzyme
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x * 56560, SDS-PAGE
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?
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x * 48000, SDS-PAGE
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?
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x * 64000, SDS-PAGE
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?
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x * 47000, SDS-PAGE
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?
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x * 35100, isoenzyme C2, SDS-PAGE, x * 36800, isoenzyme C4, SDS-PAGE, x * 37000, isoenzyme C1, SDS-PAGE, x * 38200, isoenzyme C3, SDS-PAGE, x * 30400, isoenzyme A, SDS-PAGE, x * 32700, isoenzyme B, SDS-PAGE
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x * 25000, SDS-PAGE in presence of beta-mercaptoethanol, PLC-A,x * 29000, SDS-PAGE in presence of beta-mercaptoethanol, PLC-B
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x * 44900, SDS-PAGE
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?
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x * 33100, isoenzyme I, SDS-PAGE, x * 36200, isoenzyme II, SDS-PAGE, x * 39000, isoenzyme III, SDS-PAGE
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x * 53500, recombinant enzyme, SDS-PAGE
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x * 53500, recombinant enzyme, SDS-PAGE
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?
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x * 40000, SDS-PAGE
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x * 39700, calculated from sequence
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x * 71365, truncated ChiA mutant enzyme ChiADELTACtBM, sequence calculation
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Salmonella enterica typhimurium SL1344
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x * 71365, truncated ChiA mutant enzyme ChiADELTACtBM, sequence calculation
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?
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x * 54000 + x * 46000, SDS-PAGE, chitinase from stomach extracts
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x * 52000 + x * 58000, SDS-PAGE
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x * 62000, recombinant His6-tagged enzyme, SDS-PAGE
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x * 62000, recombinant His6-tagged enzyme, SDS-PAGE
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x * 65000-70000, the enzyme appears as doublet of protein bands on SDS-PAGE at 65000-70000 Da
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x * 52000, SDS-PAGE
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x * 50000, SDS-PAGE
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x * 29000, ChiA, SDS-PAGE, x * 28789, sequence calculation
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x * 29000, ChiA, SDS-PAGE, x * 28789, sequence calculation
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?
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x * 26000, isozyme 1, SDS-PAGE, x * 43000, isozyme 2, SDS-PAGE
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x * 26000, isozyme 1, SDS-PAGE, x * 43000, isozyme 2, SDS-PAGE
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?
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x * 32000, SDS-PAGE
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x * 32000 + x * 37000, SDS-PAGE
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x * 32000 + x * 37000, SDS-PAGE
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x * 20000, SDS-PAGE
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?
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x * 66000, SDS-PAGE
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x * 48400, SDS-PAGE, x * 43800, calculated
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x * 44900, SDS-PAGE
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Thermochaetoides thermophila
x * 47300, SDS-PAGE
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Thermochaetoides thermophila
x * 47300, SDS-PAGE, x * 45100, calculated
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x * 134259, deduced from amino acid sequence
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x * 111000, calculated from amino acid sequence and SDS-PAGE
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x * 46370, calculated from amino acid sequence
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x * 49400, recombinant His6-tagged enzyme, SDS-PAGE
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x * 46000, SDS-PAGE, x * 42265, Chi46, amino acid sequence calculation
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x * 46000, SDS-PAGE, x * 42265, Chi46, amino acid sequence calculation
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x * 45300, calculated from amino acid sequence
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x * 46000, SDS-PAGE
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x * 114000, His-tagged enzyme, SDS-PAGE
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x * 62200, His-tagged enzyme, calculated from amino acid sequence
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x * 114000, His-tagged enzyme, SDS-PAGE
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?
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x * 62200, His-tagged enzyme, calculated from amino acid sequence
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?
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x * 63770, recombinant His6-tagged chitinase A 575 amino acid fragment, mass spectrometry
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x * 87396, calculated from sequence
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x * 87396, calculated from sequence
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x * 31000, SDS-PAGE
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dimer
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2 * 15800, SDS-PAGE
dimer
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2 * 36000, ChiA, SDS-PAGE
dimer
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2 * 36000, ChiA, SDS-PAGE
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dimer
2 * 77000, SDS-PAGE
dimer
2 * 77700, calculated from sequence
homodimer
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2 * 38000, SDS-PAGE
homodimer
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2 * 38000, SDS-PAGE
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monomer
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1 * 14310, SDS-PAGE, 1 * 14309, mass spectrometry
monomer
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1 * 45000, endochitinase-1, SDS-PAGE
monomer
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1 * 51000, endochitinase-2, SDS-PAGE
monomer
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1 * 45000, endochitinase-1, SDS-PAGE
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monomer
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1 * 51000, endochitinase-2, SDS-PAGE
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monomer
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1 * 35500, SDS-PAGE
monomer
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1 * 35000, SDS-PAGE
monomer
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1 * 35000, SDS-PAGE
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monomer
1 * 65000, recombinant His-tagged enzyme, SDS-PAGE
monomer
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1 * 65000, recombinant His-tagged enzyme, SDS-PAGE
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monomer
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1 * 35000, SDS-PAGE
monomer
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1 * 36500, SDS-PAGE
monomer
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1 * 36500, SDS-PAGE
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monomer
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1 * 35000, SDS-PAGE
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monomer
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1 * 29000, PAGE and SDS-PAGE
monomer
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1 * 77000, chitinase 1, SDS-PAGE
monomer
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1 * 98000, chitinase 2, SDS-PAGE
monomer
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1 * 30000, SDS-PAGE
monomer
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1 * 59000, SDS-PAGE
monomer
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1 * 59103, MALDI-TOF mass spectrometry
monomer
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1 * 59000, SDS-PAGE
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monomer
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1 * 59103, MALDI-TOF mass spectrometry
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monomer
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1 * 56000, isoform Chi-560, SDS-PAGE
monomer
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1 * 45000, SDS-PAGE
monomer
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1 * 45201, calculated from amino acid sequence
monomer
-
1 * 45000, SDS-PAGE
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monomer
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1 * 45201, calculated from amino acid sequence
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monomer
1 * 60788, Chi60, sequence calculation
monomer
-
1 * 34000, SDS-PAGE
monomer
-
1 * 75000, SDS-PAGE
monomer
1 * 70000, SDS-PAGE
monomer
1 * 67000, SDS-PAGE
monomer
1 * 70100, calculated from amino acid sequence
monomer
-
1 * 70000, SDS-PAGE
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monomer
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1 * 70100, calculated from amino acid sequence
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monomer
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1 * 67000, SDS-PAGE
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monomer
1 * 150000, about, chitinase ChiW, sequence calculation, 1 * 130000, recombinant truncated His-tagged enzyme, specifically cleaved between Asn282 and Ser283 during the purification step, the resulting two polypeptide fragments were non-covalently bound, SDS-PAGE
monomer
-
1 * 28600, SDS-PAGE
monomer
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1 * 30600, SDS-PAGE
monomer
-
1 * 68000, CHT1, SDS-PAGE
monomer
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1 * 68000, CHT1, SDS-PAGE
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monomer
1 * 44600, SDS-PAGE, 1 * 44709, calculated
monomer
-
1 * 50103, mass spectrometry, 1 * 50000, SDS-PAGE
monomer
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1 * 29000, SDS-PAGE
monomer
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1 * 29000, SDS-PAGE
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monomer
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1 * 65000, SDS-PAGE
monomer
-
1 * 65000, SDS-PAGE
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monomer
-
1 * 44000, SDS-PAGE
monomer
-
1 * 70000, SDS-PAGE
monomer
-
1 * 48000, SDS-PAGE
monomer
-
1 * 48000, SDS-PAGE
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monomer
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1 * 30000, SDS-PAGE
monomer
1 * 60000, SDS-PAGE
monomer
1 * 60088, calculated from sequence
additional information
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peptide mapping by MALDI-TOF mass spectroemtry
additional information
Q0WT03
AtChiC adopts an (beta/alpha)8 fold with a small insertion domain composed of an alpha-helix and a five-stranded beta-sheet, secondary structure comparison, overview
additional information
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AtChiC adopts an (beta/alpha)8 fold with a small insertion domain composed of an alpha-helix and a five-stranded beta-sheet, secondary structure comparison, overview
additional information
ChiA consists of a signal sequence, a region including chitinase consensus motifs, a Ser/Thr/Pro-rich region and a glycosylphosphatidylinositol-anchor attachment motif
additional information
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ChiA consists of a signal sequence, a region including chitinase consensus motifs, a Ser/Thr/Pro-rich region and a glycosylphosphatidylinositol-anchor attachment motif
additional information
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ChiA consists of a signal sequence, a region including chitinase consensus motifs, a Ser/Thr/Pro-rich region and a glycosylphosphatidylinositol-anchor attachment motif
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additional information
determination of the primary structure by mass spectrometry, sequence comparisons, overview
additional information
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tryptic peptide mapping and comparison with the exochitinase from Bacillus cereus ATCC14579
additional information
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tryptic peptide mapping and comparison with the exochitinase from Bacillus cereus ATCC14579
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additional information
enzyme consists of a catalytic domain, a fibronectin type III domain , and a chitin binding domain. The catalytic domain with one amino acid in C-terminal region is sufficient for chitinase activity. The C-terminus is important in binduing to shell powder
additional information
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enzyme consists of a catalytic domain, a fibronectin type III domain , and a chitin binding domain. The catalytic domain with one amino acid in C-terminal region is sufficient for chitinase activity. The C-terminus is important in binduing to shell powder
additional information
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structural characterization of the enzyme
additional information
isozyme domain structures, overview
additional information
isozyme domain structures, overview
additional information
isozyme domain structures, overview
additional information
isozyme domain structures, overview
additional information
isozyme domain structures, overview
additional information
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isozyme domain structures, overview
additional information
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isozyme domain structures, overview
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additional information
CrChi1 has the DXDXE motif at the end of strand beta5, with Glu174 as the catalytic residue in the middle of the open end of the (beta/alpha)8 barrel
additional information
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CrChi1 has the DXDXE motif at the end of strand beta5, with Glu174 as the catalytic residue in the middle of the open end of the (beta/alpha)8 barrel
additional information
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the secondary sturcture contains a repeat structure near the N-terminus exhibiting polymorphism between isolates dependent on repeat copy number
additional information
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the secondary structure contains a repeat structure near the N-terminus exhibiting polymorphism between isolates dependent on repeat copy number
additional information
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BcChi-A is glycoside hydrolase family-19 chitinase lacking loops I, II, IV and V, and a C-terminal loop, which are present in the catalytic domain of plant class I and II chitinases
additional information
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SI-CLP is lacking the chitin-binding domain
additional information
three-dimensional structure modelling using the crystal structure of the human chitotriosidase, EC 3.2.1.44, PDB ID 1HKK, and the molecular mechanics and molecular dynamics methods, overview
additional information
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three-dimensional structure modelling using the crystal structure of the human chitotriosidase, EC 3.2.1.44, PDB ID 1HKK, and the molecular mechanics and molecular dynamics methods, overview
additional information
determination of the primary structure by mass spectrometry, sequence comparisons, overview
additional information
determination of the primary structure by mass spectrometry, sequence comparisons, overview
additional information
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determination of the primary structure by mass spectrometry, sequence comparisons, overview
additional information
molecular dynamics simulations of wild-type and mutant enzymes, overview
additional information
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molecular dynamics simulations of wild-type and mutant enzymes, overview
additional information
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the enzyme has a chitin-binding domain and a fibronectin type 3-like domain in the N-terminal region, molecular domain structure, comparisons, overview
additional information
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the enzyme has a chitin-binding domain and a fibronectin type 3-like domain in the N-terminal region, molecular domain structure, comparisons, overview
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additional information
Chi60 domain structure, overview
additional information
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Chi60 domain structure, overview
additional information
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the chitin-binding domain ChBD comprises 45 amino acid residues and exhibits high specificity for chitin
additional information
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the chitin-binding domain ChBD comprises 45 amino acid residues, a tightly packed structure, and exhibits high specificity for and stable binding to chitin
additional information
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the chitin-binding domain ChBD comprises 45 amino acid residues, a tightly packed structure, and exhibits high specificity for and stable binding to chitin
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additional information
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the chitin-binding domain ChBD comprises 45 amino acid residues and exhibits high specificity for chitin
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additional information
enzyme NtChiV adopts a classical (beta/alpha)8-barrel fold, residues 1-233 and 303-348, with an insertion of a small, alpha + beta, domain, residues 234-302. The chitin-binding domain is present in the C-terminus
additional information
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enzyme NtChiV adopts a classical (beta/alpha)8-barrel fold, residues 1-233 and 303-348, with an insertion of a small, alpha + beta, domain, residues 234-302. The chitin-binding domain is present in the C-terminus
additional information
the enzyme contains an anchoring domains in the N-terminus and two catalytic domains at the C-terminal region, presence of a beta-stranded-rich structure in the N-terminus
additional information
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the enzyme contains an anchoring domains in the N-terminus and two catalytic domains at the C-terminal region, presence of a beta-stranded-rich structure in the N-terminus
additional information
secondary structure analysis, peptide mapping
additional information
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secondary structure analysis, peptide mapping
additional information
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secondary structure analysis, peptide mapping
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additional information
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multi-domain structure are the domain (D132-A155) where the active site is located, and the domain (A437-W479) that includes a C-terminal carbohydrate-binding module 5
additional information
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multi-domain structure are the domain (D132-A155) where the active site is located, and the domain (A437-W479) that includes a C-terminal carbohydrate-binding module 5
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additional information
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peptide mass mapping, overview
additional information
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peptide mass mapping, overview
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additional information
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the chitinase has unique structural features and contains two catalytic domains AD1 and AD2 and two chitin-binding domains ChBD1 and ChBD2. ChBD2 consists of two four-stranded beta-sheets and is composed of a typical beta-sandwich architecture, tertiary structure by NMR and crystal structure determinations, overview
additional information
determination of the primary structure by mass spectrometry, sequence comparisons, overview
additional information
determination of the primary structure by mass spectrometry, sequence comparisons, overview
additional information
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determination of the primary structure by mass spectrometry, sequence comparisons, overview
additional information
-
-
additional information
the catalytic domain has a TIM-barrel fold, structure modelling, overview
additional information
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the catalytic domain has a TIM-barrel fold, structure modelling, overview
additional information
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enzyme peptide mapping, overview
additional information
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enzyme peptide mapping, overview
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additional information
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the enzyme sequence contains a pre-pro type signal peptide
additional information
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the enzyme sequence contains a pre-pro type signal peptide
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additional information
determination of the primary structure by mass spectrometry, sequence comparisons, overview
additional information
determination of the primary structure by mass spectrometry, sequence comparisons, overview
additional information
determination of the primary structure by mass spectrometry, sequence comparisons, overview
additional information
determination of the primary structure by mass spectrometry, sequence comparisons, overview
additional information
determination of the primary structure by mass spectrometry, sequence comparisons, overview
additional information
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determination of the primary structure by mass spectrometry, sequence comparisons, overview
additional information
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three distinct domains: 1. the amino-terminal chitin-binding domain, 2. the main catalytic (alpha/beta)8 TIM-barrel domain, and 3. the small (alpha + beta) insertion domain. The catalytic cleft of chitinase A has a long, deep groove, which contains six chitooligosaccharide ring-binding subsites, overview
additional information
tryptic peptide mapping and mass spectrometric analysis
additional information
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tryptic peptide mapping and mass spectrometric analysis
additional information
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tryptic peptide mapping and mass spectrometric analysis
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