Literature summary for 3.5.3.11 extracted from

Kim, K.H.; Ahn, H.J.; Kim, D.J.; Lee, H.H.; Ha, J.Y.; Kim, H.K.; Yoon, H.J.; Suh, S.W.
Expression, crystallization and preliminary X-ray crystallographic analysis of human agmatinase (2005), Acta Crystallogr. Sect. F, 61, 889-891.

Cloned(Commentary)

Cloned (Comment)	Organism
residues Ala36-Val352 overexpressed as a fusion with both N- and C-terminal purification tags in Escherichia coli	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging-drop vapour-diffusion method, agmatinase (residues Ala36-Val352) overexpressed as a fusion with both N- and C-terminal purification tags in Escherichia coli and crystallized in the presence of Mn2+ and 1,6-diaminohexane at 297 K using polyethylene glycol 4000 as a precipitant. X-ray diffraction data are collected at 100 K to 2.49 A from a flash-frozen crystal. The crystals are tetragonal, belonging to space group P4(2), with unit-cell parameters a = b = 114.54 A, c =125.65A, alpha = beta = gamma = 90°. Three monomers are likely to be present in the asymmetric unit, giving a crystal volume per protein weight of 3.66A	Homo sapiens

Crystallization (Comment)

Organism

hanging-drop vapour-diffusion method, agmatinase (residues Ala36-Val352) overexpressed as a fusion with both N- and C-terminal purification tags in Escherichia coli and crystallized in the presence of Mn2+ and 1,6-diaminohexane at 297 K using polyethylene glycol 4000 as a precipitant. X-ray diffraction data are collected at 100 K to 2.49 A from a flash-frozen crystal. The crystals are tetragonal, belonging to space group P4(2), with unit-cell parameters a = b = 114.54 A, c =125.65A, alpha = beta = gamma = 90°. Three monomers are likely to be present in the asymmetric unit, giving a crystal volume per protein weight of 3.66A

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Homo sapiens

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)