Camel and bovine chymosin: the relationship between their structures and cheese-making properties

Langholm Jensen, J.; Mølgaard, A.; Navarro Poulsen, J.-C.; Harboe, M.K.; Simonsen, J.B.; Lorentzen, A.M.; Hjernø, K.; van den Brink, J.M.; Qvist, K.B.; Larsen, S.

doi:10.1107/S0907444913003260

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 5
The substrate-binding clefts of bovine (a, c) and camel (b, d) chymosin. The active-site residues and the activated water molecule are illustrated in red. Residues 11–16 of camel chymosin are shown in magenta. Glycerol (Gol1334) and the residues that differ between bovine and camel chymosin are shown in green (Table 4

). (a) and (b) illustrate the loops that form the entrance to the binding site. (c) Subsite S1 with Leu32 and subsites S2 and S4 with Lys221 and Val223. (d) The corresponding subsites in camel chymosin with Val32 (both conformations) and with Val221 and Phe223, respectively.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 69| Part 5| April 2013| Pages 901-913

doi:10.1107/S0907444913003260

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