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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
Acylphosphatase
Structure of acylphosphatase.
[2] Symbol Acylphosphatase Pfam PF00708 InterPro IPR001792 PROSITE PDOC00136 SCOP2 1aps / SCOPe / SUPFAM
Pfam
structures / ECOD
PDB RCSB PDB ; PDBe ; PDBj PDBsum structure summary PDB 2GV1 1APS 2FHM 1Y9O 1URR 1W2I 2ACY 2BJD 1V3Z 2HLT 2HLU 2BJE 3BR8 1ULR
In enzymology , an acylphosphatase (EC 3.6.1.7 ) is an enzyme that catalyzes the hydrolysis of the carboxyl-phosphate bond of acylphosphates, with acylphosphate and H 2 O substrates of this enzyme, and carboxylate and phosphate as its two products :[3]
Function [ edit ]
This enzyme belongs to the family of hydrolases , specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is acylphosphate phosphohydrolase . Other names in common use include acetylphosphatase , 1,3-diphosphoglycerate phosphatase , acetic phosphatase , Ho 1-3 , and GP 1-3 .
This enzyme participates in 3 metabolic pathways :
Structural studies [ edit ]
Structures of this enzyme have been solved by both NMR and X-ray crystallography . See the links to PDB structures in the info boxes on the right for a current list of structures available in the PDB . The protein contains a beta sheet stacked on two alpha helices described by CATH as an Alpha-Beta Plait fold. The active site sits between sheet and helices and contains an arginine and an asparagine.[4] [5]
Isozymes [ edit ]
Humans express the following two acylphosphatase isozymes:
References [ edit ]
^ Pastore A, Saudek V, Ramponi G, Williams RJ (March 1992). "Three-dimensional structure of acylphosphatase. Refinement and structure analysis". J. Mol. Biol . 224 (2 ): 427–40. doi :10.1016/0022-2836(92 )91005-A . PMID 1313885 .
^ Stefani M, Taddei N, Ramponi G (February 1997). "Insights into acylphosphatase structure and catalytic mechanism" . Cell. Mol. Life Sci . 53 2 ): 141–51. doi :10.1007/PL00000585 . PMC 11147357 PMID 9118002 . S2CID 24072481 .
^ Gribenko AV, Patel MM, Liu J, McCallum SA, Wang C, Makhatadze GI (February 2009). "Rational stabilization of enzymes by computational redesign of surface charge-charge interactions" . Proceedings of the National Academy of Sciences of the United States of America . 106 (8 ): 2601–6. Bibcode :2009PNAS..106.2601G . doi :10.1073/pnas.0808220106 PMC 2650310 PMID 19196981 .
^ "Enzyme 3.6.1.7" . PDBe Enzyme Browser .
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Activity
Regulation
Classification
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R e t r i e v e d f r o m " https://en.wikipedia.org/w/index.php?title=Acylphosphatase&oldid=1228268133 " C a t e g o r i e s : ● G e n e s o n h u m a n c h r o m o s o m e 1 4 ● G e n e s o n h u m a n c h r o m o s o m e 2 ● E C 3 . 6 . 1 ● E n z y m e s o f k n o w n s t r u c t u r e ● E C 3 . 6 s t u b s H i d d e n c a t e g o r i e s : ● A r t i c l e s w i t h s h o r t d e s c r i p t i o n ● S h o r t d e s c r i p t i o n m a t c h e s W i k i d a t a ● 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 ● A l l s t u b a r t i c l e s
● T h i s p a g e w a s l a s t e d i t e d o n 1 0 J u n e 2 0 2 4 , a t 0 9 : 1 9 ( 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
