2VH7

Crystal structure of human common-type acylphosphatase

Summary for 2VH7

Entry DOI	10.2210/pdb2vh7/pdb
Descriptor	ACYLPHOSPHATASE-1 (2 entities in total)
Functional Keywords	hydrolase, acetylation
Biological source	HOMO SAPIENS (HUMAN)
Total number of polymer chains	1
Total formula weight	11277.84
Authors	Yeung, R.C.Y.,Lam, Y.,Wong, K.B. (deposition date: 2007-11-19, release date: 2009-03-17, Last modification date: 2023-12-13)
Primary citation	Lam, S.Y.,Yeung, R.C.Y.,Yu, T.,Sze, K.,Wong, K.B. A Rigidifying Salt-Bridge Favors the Activity of Thermophilic Enzyme at High Temperatures at the Expense of Low-Temperature Activity. Plos Biol., 9:1027-, 2011 Cited by PubMed Abstract: Thermophilic enzymes are often less active than their mesophilic homologues at low temperatures. One hypothesis to explain this observation is that the extra stabilizing interactions increase the rigidity of thermophilic enzymes and hence reduce their activity. Here we employed a thermophilic acylphosphatase from Pyrococcus horikoshii and its homologous mesophilic acylphosphatase from human as a model to study how local rigidity of an active-site residue affects the enzymatic activity. PubMed: 21423654 DOI: 10.1371/JOURNAL.PBIO.1001027 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.45 Å)

Structure validation