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? * 125000, zeta, SDS-PAGE
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? * 68000, alpha, SDS-PAGE
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? * 79000, gamma, SDS-PAGE
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? * 110000, delta, SDS-PAGE
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? * 115000, beta, SDS-PAGE
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? * 76000, C3, SDS-PAGE
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? * 92000, C2, SDS-PAGE
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? * 96000, C1, SDS-PAGE
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x * 113866, mass spectrometry, full length enzyme containing two collagen-binding domains
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x * 35000, SDS-PAGE
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monomer
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1 * 72000, IIIb, SDS-PAGE
monomer
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1 * 81000, I, II, IIIa, SDS-PAGE
monomer
1 * 114000, calculated
monomer
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1 * 75000, no dissociation into subunits after lithium chloride treatment, SDS-PAGE
monomer
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1 * 64000, SDS-PAGE
tetramer
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x * 24000 + x * 28000, SDS-PAGE after denaturation with SDS and beta-mercaptoethanol
tetramer
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x * 24000 + x * 28000, SDS-PAGE after denaturation with SDS and beta-mercaptoethanol
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additional information
enzyme domain structure, overview
additional information
enzyme domain structure, overview
additional information
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enzyme domain structure, overview
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additional information
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enzyme domain structure, overview
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additional information
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enzyme domain structure, overview
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additional information
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enzyme domain structure, overview
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additional information
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enzyme domain structure, overview
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additional information
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enzyme domain structure, overview
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additional information
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enzyme domain structure, overview
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additional information
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enzyme domain structure, overview
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additional information
enzyme domain structure, overview. Enzyme ColA possesses segments S1, S2, S3a, and S3b. In ColA, S3 is composed by a tandem repeated structure (S3a and S3b) that enhances binding to collagen, this is characteristic of class I collagenases
additional information
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enzyme domain structure, overview. Enzyme ColA possesses segments S1, S2, S3a, and S3b. In ColA, S3 is composed by a tandem repeated structure (S3a and S3b) that enhances binding to collagen, this is characteristic of class I collagenases
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additional information
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enzyme domain structure, overview. Enzyme ColA possesses segments S1, S2, S3a, and S3b. In ColA, S3 is composed by a tandem repeated structure (S3a and S3b) that enhances binding to collagen, this is characteristic of class I collagenases
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additional information
the enzyme consists of a signal sequence for secretion, a prosequence for maturation, a catalytic region, 14 direct repeats of 20 amino acids at the C terminus, and a region with unknown function intervening between the catalytic region and the numerous repeats
additional information
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the enzyme consists of a signal sequence for secretion, a prosequence for maturation, a catalytic region, 14 direct repeats of 20 amino acids at the C terminus, and a region with unknown function intervening between the catalytic region and the numerous repeats
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additional information
ColG possesses a single PKD-like domain and a duplicated CBD domain in addition to the catalytic domain, comprising residues Tyr119-Ala790
additional information
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ColG possesses a single PKD-like domain and a duplicated CBD domain in addition to the catalytic domain, comprising residues Tyr119-Ala790
additional information
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enzyme exists in two isoforms differing in the presence of one or two collagen-binding domains of 12 amino acids, respectively
additional information
isoform ColG consists of a collagenase module s1, polycystic kidney disease-like (PKD-like) domain s2 and collagen-binding domains s3a and s3b
additional information
isoform ColG consists of a collagenase module s1, polycystic kidney disease-like (PKD-like) domain s2 and collagen-binding domains s3a and s3b
additional information
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isoform ColG consists of a collagenase module s1, polycystic kidney disease-like (PKD-like) domain s2 and collagen-binding domains s3a and s3b
additional information
isoform ColH consists of a collagenase module s1, polycystic kidney disease-like (PKD-like) domains s2a and s2b and collagen-binding domain s3
additional information
isoform ColH consists of a collagenase module s1, polycystic kidney disease-like (PKD-like) domains s2a and s2b and collagen-binding domain s3
additional information
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isoform ColH consists of a collagenase module s1, polycystic kidney disease-like (PKD-like) domains s2a and s2b and collagen-binding domain s3
additional information
Clostridium histolyticum class II collagenase (ColH) contains two polycystic kidney disease (PKD) domains and one collagenbinding domain (CBD), which are necessary for the catalytic activity and collagen-binding affinity of this enzyme
additional information
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Clostridium histolyticum class II collagenase (ColH) contains two polycystic kidney disease (PKD) domains and one collagenbinding domain (CBD), which are necessary for the catalytic activity and collagen-binding affinity of this enzyme
additional information
enzyme domain structure, overview. Enzyme ColH possesses segments S1, S2a, S2b, and S3
additional information
enzyme domain structure, overview. Enzyme ColH possesses segments S1, S2a, S2b, and S3
additional information
enzyme domain structure, overview. In ColG, S3 is composed by a tandem repeated structure (S3a and S3b) that enhances binding to collagen, this is characteristic of class I collagenases. ColG functional domains: (i) the CBD(s) that locate and anchor the enzyme to collagen by specifically recognizing their triplehelical conformation. ColG CBDs promote interaction with fibrils, not with individual triple helices; (ii) the PKD-like domain(s) swell and prepare the substrate without triple helix unwinding; and (iii) the collagenase unit degrades the prepared collagen molecules, digesting them from microfibrils of 35A diameter downwards
additional information
enzyme domain structure, overview. In ColG, S3 is composed by a tandem repeated structure (S3a and S3b) that enhances binding to collagen, this is characteristic of class I collagenases. ColG functional domains: (i) the CBD(s) that locate and anchor the enzyme to collagen by specifically recognizing their triplehelical conformation. ColG CBDs promote interaction with fibrils, not with individual triple helices; (ii) the PKD-like domain(s) swell and prepare the substrate without triple helix unwinding; and (iii) the collagenase unit degrades the prepared collagen molecules, digesting them from microfibrils of 35A diameter downwards
additional information
the S1 domain is the catalytic segment containing the sequence HEXXH, a group of amino acids that constitute the catalytic center. S2 is one extra domain, and segments S3a and S3b work together forming a union. Enzyme domain structure, overview
additional information
the S1 domain is the catalytic segment containing the sequence HEXXH, a group of amino acids that constitute the catalytic center. S2 is one extra domain, and segments S3a and S3b work together forming a union. Enzyme domain structure, overview
additional information
enzyme domain structure, overview. M09.001 enzymes exhibit a peptidase M9N domain, a peptidase M9 domain, a PKD-like domain and/or a bacterial pre-peptidase C-terminal domain (PPC)
additional information
enzyme domain structure, overview. In peptidases from subfamily type M09.004, the PKD-like domain and the bacterial PPC are absent, resulting in lower molecular mass enzymes
additional information
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enzyme domain structure, overview. In peptidases from subfamily type M09.004, the PKD-like domain and the bacterial PPC are absent, resulting in lower molecular mass enzymes
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additional information
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enzyme domain structure, overview. In peptidases from subfamily type M09.004, the PKD-like domain and the bacterial PPC are absent, resulting in lower molecular mass enzymes
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additional information
enzyme domain structure, overview. In peptidases from subfamily type M09.004, the PKD-like domain and the bacterial PPC are absent, resulting in lower molecular mass enzymes
additional information
enzyme domain structure, overview. M09.001 enzymes exhibit a peptidase M9N domain, a peptidase M9 domain, a PKD-like domain and/or a bacterial pre-peptidase C-terminal domain (PPC)
additional information
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enzyme domain structure, overview. M09.001 enzymes exhibit a peptidase M9N domain, a peptidase M9 domain, a PKD-like domain and/or a bacterial pre-peptidase C-terminal domain (PPC)
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additional information
enzyme domain structure, overview. In peptidases from subfamily type M09.004, the PKD-like domain and the bacterial PPC are absent, resulting in lower molecular mass enzymes