1.14.99.56: lytic cellulose monooxygenase (C4-dehydrogenating)
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For detailed information about lytic cellulose monooxygenase (C4-dehydrogenating), go to the full flat file.
Reaction
Synonyms
AA9, AA9A, Cel61a, chitin-binding domain 3 protein, FG02202.1, gh61-5, gh61e, GH61I, LPMO-02916, LPMO10B, LPMO9A, LPMO9C, LPMO9E, LPMO9f, LPMO9I, Micau_1630, NCU08760, Pte6, SCO0643, Tfu_1268
ECTree
1.14.99.56 lytic cellulose monooxygenase (C4-dehydrogenating)Advanced search results
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results (Crystallization
Crystallization on EC 1.14.99.56 - lytic cellulose monooxygenase (C4-dehydrogenating)
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CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
structure of the catalytic domain, residues 37-230, to 1.08 A resolution. The active site in is formed by residues His-37 and His-144 that coordinate the copper atom in a T-shaped geometry
structure of AA9A bound to cellulosic and non-cellulosic oligosaccharides
substrate cellohexaose binds to subsites ?4 to +2, and cellotriose from subsites -1 to +2. Residue Tyr203 is placed approximately 15 A away from the copper active site
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structure of the catalytic domain, residues 37-230, to 1.08 A resolution. The active site in is formed by residues His-37 and His-144 that coordinate the copper atom in a T-shaped geometry
hybrid quantum mechanics and molecular mechanics investigation of the first steps of the LPMO mechanism, which is reduction of Cu(II) to Cu(I) and the formation of a Cu(II)-superoxide complex. In the complex, the superoxide can bind either in an equatorial or an axial position. The equatorial isomer of the superoxide complex is over 60 kJ/mol more stable than the axial isomer because it is stabilized by interactions with a second-coordination-sphere glutamine residue
comparison of isoforms LPMO9A, LPMO9B and LPMO9C. LPMO9B contains distal from the coordinated copper sphere an additional loop (Gly115-Asn121), which is not present in LPMO9A and LPMO9C. The copper ion in LPMO9A, LPMO9B and LPMO9C is coordinated by His1-His68-Tyr153, His1-His79-Tyr170 and His1-His84-Tyr166, respectively. All three LPMOs share two putative disulfide bridges
