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Literature summary for 3.4.21.47 extracted from

  • Ponnuraj, K.; Xu, Y.; Macon, K.; Moore, D.; Volanakis, J.E.; Narayana, S.V.
    Structural analysis of engineered Bb fragment of complement factor B: insights into the activation mechanism of the alternative pathway C3-convertase (2004), Mol. Cell, 14, 17-28.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
engineered subunit Bb with Cys-resiudes at positions 435 and 428, in complex with inhibitors 6-amidino-2-naphthyl-4-guanidinobenzoate or diisopropyl phosphate Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information introduction of Cys-residues to form a disulfide bond at positions 428 and 435 of von Willebrandt factor type A domain of subunit Bb. Adaption of an active conformation by the domain, which is not sufficient to activate the enzyme catalytic apparatus Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
6-amidino-2-naphthyl-4-guanidinobenzoate
-
Homo sapiens
diisopropyl phosphate
-
Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.75
-
t-butyloxycarbonyl-Gly-L-Leu-L-Ala-L-Arg-thiobenzyl ester subunit Bb, mutant with Cys-residues at positions 428, 435 Homo sapiens
5.63
-
t-butyloxycarbonyl-Gly-L-Leu-L-Ala-L-Arg-thiobenzyl ester subunit Bb, wild-type Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P00751
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
t-butyloxycarbonyl-Gly-L-Leu-L-Ala-L-Arg-thiobenzyl ester substrate of enzyme subunit Bb Homo sapiens ?
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.28
-
t-butyloxycarbonyl-Gly-L-Leu-L-Ala-L-Arg-thiobenzyl ester subunit Bb, mutant with Cys-residues at positions 428, 435 Homo sapiens
0.65
-
t-butyloxycarbonyl-Gly-L-Leu-L-Ala-L-Arg-thiobenzyl ester subunit Bb, wild-type Homo sapiens