Crystallization and preliminary X-ray diffraction analysis of the amidase domain of allophanate hydrolase from Pseudomonas sp. strain ADP

Balotra, S.; Newman, J.; French, N.G.; Briggs, L.J.; Peat, T.S.; Scott, C.

doi:10.1107/S2053230X13034705

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

IUCr IT WDC

home archive editors for authors for readers submit subscribe open access

view article

Figure 1
Catabolic processes involving allophanate hydrolase (AH). The cyanuric acid catabolic pathway involves ring opening of cyanuric acid by cyanuric acid hydrolase (CH), spontaneous decarboxylation of the product (1-carboxybiuret) and deamination of biuret by biuret hydrolase (BH) to produce allophanate. The urea catabolic pathway involves ATP-dependent urea carboxylation by urea carboxylase (UC) to produce allophanate. Both pathways then depend upon allophanate deamination by allophanate hydrolase to avoid spontaneous decarboxylation (and urea formation).

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 70| Part 3| February 2014| Pages 310-315

doi:10.1107/S2053230X13034705

Follow Acta Cryst. F

Search term		doi		Advanced search
Author		volume	page