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P a g e s f o r l o g g e d o u t e d i t o r s l e a r n m o r e ● C o n t r i b u t i o n s ● T a l k
( T o p )
1 E n z y m e s
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F r o m W i k i p e d i a , t h e f r e e e n c y c l o p e d i a
Enzymes
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Arginase
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Arginase , which catalyses the conversion of arginine to urea and ornithine , is one of the five members of the urea cycle enzymes that convert ammonia to urea as the principal product of nitrogen excretion.[5] argininemia , which is usually associated with hyperammonemia .
Agmatinase
[ edit ]
Agmatinase hydrolyses agmatine to putrescine , the precursor for the biosynthesis of higher polyamines , spermidine and spermine . In addition, agmatine may play an important regulatory role in mammals.[6]
[ edit ]
Formiminoglutamase catalyses the fourth step in histidine degradation, acting to hydrolyse N L L formamide .
Proclavaminate amidinohydrolase
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Proclavaminate amidinohydrolase is involved in clavulanic acid biosynthesis. Clavulanic acid acts as an inhibitor of a wide range of beta-lactamase enzymes that are used by various microorganisms to resist beta-lactam antibiotics. As a result, this enzyme improves the effectiveness of beta-lactamase antibiotics.[4] [7]
References
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^ Christianson DW , Di Costanzo L, Sabio G, Mora A, Rodriguez PC, Ochoa AC, Centeno F (2005). "Crystal structure of human arginase I at 1.29-A resolution and exploration of inhibition in the immune response" . Proc. Natl. Acad. Sci. U.S.A . 102 (37 ): 13058–13063. doi :10.1073/pnas.0504027102 PMC 1201588 PMID 16141327 .
^ a b Clifton IJ, Elkins JM, Hernandez H (2002). "Oligomeric structure of proclavaminic acid amidino hydrolase: evolution of a hydrolytic enzyme in clavulanic acid biosynthesis" . Biochem. J . 366 (Pt 2): 423–434. doi :10.1042/BJ20020125 . PMC 1222790 PMID 12020346 .
^ Baker BS , Tata JR, Xu Q (1993). "Developmental and hormonal regulation of the Xenopus liver-type arginase gene" . Eur. J. Biochem . 211 (3 ): 891–898. doi :10.1111/j.1432-1033.1993.tb17622.x PMID 7916684 .
^ Ahn HJ, Kim KH, Lee J, et al. (November 2004). "Crystal structure of agmatinase reveals structural conservation and inhibition mechanism of the ureohydrolase superfamily" . J. Biol. Chem . 279 (48 ): 50505–13. doi :10.1074/jbc.M409246200 PMID 15355972 .
^ "IPR006035 Ureohydrolase" . Retrieved 2009-02-17 .
R e t r i e v e d f r o m " https://en.wikipedia.org/w/index.php?title=Ureohydrolase&oldid=1214484700 " C a t e g o r y : ● H y d r o l a s e s H i d d e n c a t e g o r y : ● P r o t e i n p a g e s n e e d i n g a p i c t u r e
● T h i s p a g e w a s l a s t e d i t e d o n 1 9 M a r c h 2 0 2 4 , a t 0 7 : 0 5 ( U T C ) . ● T e x t i s a v a i l a b l e u n d e r t h e C r e a t i v e C o m m o n s A t t r i b u t i o n - S h a r e A l i k e L i c e n s e 4 . 0 ;
a d d i t i o n a l t e r m s m a y a p p l y . B y u s i n g t h i s s i t e , y o u a g r e e t o t h e T e r m s o f U s e a n d P r i v a c y P o l i c y . W i k i p e d i a ® i s a r e g i s t e r e d t r a d e m a r k o f t h e W i k i m e d i a F o u n d a t i o n , I n c . , a n o n - p r o f i t o r g a n i z a t i o n . ● P r i v a c y p o l i c y ● A b o u t W i k i p e d i a ● D i s c l a i m e r s ● C o n t a c t W i k i p e d i a ● C o d e o f C o n d u c t ● D e v e l o p e r s ● S t a t i s t i c s ● C o o k i e s t a t e m e n t ● M o b i l e v i e w
