KEGG   ENZYME: 3.1.1.77Help
Entry
EC 3.1.1.77                 Enzyme                                 

Name
acyloxyacyl hydrolase
Class
Hydrolases;
Acting on ester bonds;
Carboxylic-ester hydrolases
BRITE hierarchy
Reaction(IUBMB)
3-(acyloxy)acyl group of bacterial toxin + H2O = 3-hydroxyacyl group of bacterial toxin + a fatty acid [RN:R05792]
Reaction(KEGG)
Substrate
3-(acyloxy)acyl group of bacterial toxin [CPD:C11547];
H2O [CPD:C00001]
Product
3-hydroxyacyl group of bacterial toxin [CPD:C11548];
fatty acid [CPD:C00162]
Comment
The substrate is lipid A on the reducing end of the toxic lipopolysaccharide (LPS) of Salmonella typhimurium and related organisms. It consists of diglucosamine, beta-D-GlcN-(1-> 6)-D-GlcN, attached by glycosylation on O-6 of its non-reducing residue, phosphorylated on O-4 of this residue and on O-1 of its potentially reducing residue. Both residues carry 3-(acyloxy)acyl groups on N-2 and O-3. The enzyme from human leucocytes detoxifies the lipid by hydrolysing the secondary acyl groups from O-3 of the 3-hydroxyacyl groups on the disaccharide (LPS). It also possesses a wide range of phospholipase and acyltransferase activities [e.g. EC 3.1.1.4 (phospholipase A2), EC 3.1.1.5 (lysophospholipase), EC 3.1.1.32 (phospholipase A1) and EC 3.1.1.52 (phosphatidylinositol deacylase)], hydrolysing diacylglycerol and phosphatidyl compounds, but not triacylglycerols. It has a preference for saturated C12-C16 acyl groups.
History
EC 3.1.1.77 created 2001
Orthology
K01065  acyloxyacyl hydrolase
Genes
HSA: 313(AOAH)
PTR: 463352(AOAH)
PPS: 100994136(AOAH)
GGO: 101134942(AOAH)
PON: 100456260(AOAH)
NLE: 100585049(AOAH)
MCC: 706291(AOAH)
MCF: 102141551(AOAH)
CSAB: 103226220(AOAH)
RRO: 104660689(AOAH)
RBB: 108530681(AOAH)
CJC: 100388358(AOAH)
SBQ: 101038550(AOAH)
MMU: 27052(Aoah)
RNO: 498757(Aoah)
CGE: 100768833(Aoah)
NGI: 103743893(Aoah)
HGL: 101718171(Aoah)
CCAN: 109698614(Aoah)
OCU: 100008662(AOAH)
TUP: 102490537(AOAH)
CFA: 482402(AOAH)
AML: 100471433(AOAH)
UMR: 103658989(AOAH)
ORO: 101377931(AOAH)
FCA: 101101376(AOAH)
PTG: 102960989(AOAH)
AJU: 106968650(AOAH)
BTA: 768208(AOAH)
BOM: 102282514(AOAH)
BIU: 109557445(AOAH)
PHD: 102327820(AOAH)
CHX: 102189546(AOAH)
OAS: 101115787(AOAH)
SSC: 100522290(AOAH)
CFR: 102523361(AOAH)
CDK: 105095876(AOAH)
BACU: 103014073(AOAH)
LVE: 103075940(AOAH)
OOR: 101290037(AOAH)
ECB: 100055508(AOAH)
EPZ: 103561558(AOAH)
EAI: 106830867(AOAH)
MYB: 102260205(AOAH)
MYD: 102763366(AOAH)
HAI: 109389807(AOAH)
RSS: 109444735(AOAH)
PALE: 102893901(AOAH)
LAV: 100655055(AOAH)
TMU: 101341268
MDO: 103104605(AOAH)
SHR: 100913760 111719508(AOAH)
GGA: 420737(AOAH)
MGP: 100548243(AOAH)
CJO: 107309429(AOAH)
APLA: 101793271(AOAH)
ACYG: 106044351(AOAH)
TGU: 100230185(AOAH)
GFR: 102036558(AOAH)
FAB: 101820983(AOAH)
PHI: 102111626(AOAH)
PMAJ: 107200241(AOAH)
CCW: 104688946(AOAH)
FPG: 101918125(AOAH)
FCH: 102059809(AOAH)
CLV: 102091359(AOAH)
EGZ: 104124826(AOAH)
AAM: 106489028(AOAH)
ASN: 102373583(AOAH)
AMJ: 102570124(AOAH)
PSS: 102453660(AOAH)
CMY: 102943071(AOAH)
CPIC: 101940255(AOAH)
ACS: 100554361(aoah)
PVT: 110076184(AOAH)
PBI: 103067406(AOAH)
GJA: 107117166(AOAH)
XLA: 108719016(aoah.L)
XTR: 100491792(aoah)
NPR: 108792217(AOAH)
CIN: 100179746
SPU: 592185
TCA: 657467
ZNE: 110828349
LAK: 106172532
EPA: 110241226
ADF: 107349171
AQU: 100634015
TCR: 510289.40
 » show all
Taxonomy
Reference
1  [PMID:2398058]
  Authors
Erwin AL, Munford RS.
  Title
Deacylation of structurally diverse lipopolysaccharides by human acyloxyacyl hydrolase.
  Journal
J. Biol. Chem. 265 (1990) 16444-9.
Reference
2  [PMID:1883828]
  Authors
Hagen FS, Grant FJ, Kuijper JL, Slaughter CA, Moomaw CR, Orth K, O'Hara PJ, Munford RS.
  Title
Expression and characterization of recombinant human acyloxyacyl hydrolase, a leukocyte enzyme that deacylates bacterial lipopolysaccharides.
  Journal
Biochemistry. 30 (1991) 8415-23.
  Sequence
[hsa:313]
Reference
3  [PMID:1577781]
  Authors
Munford RS, Hunter JP.
  Title
Acyloxyacyl hydrolase, a leukocyte enzyme that deacylates bacterial lipopolysaccharides, has phospholipase, lysophospholipase, diacylglycerollipase, and acyltransferase activities in vitro.
  Journal
J. Biol. Chem. 267 (1992) 10116-21.
Other DBs
ExplorEnz - The Enzyme Database: 3.1.1.77
IUBMB Enzyme Nomenclature: 3.1.1.77
ExPASy - ENZYME nomenclature database: 3.1.1.77
BRENDA, the Enzyme Database: 3.1.1.77
CAS: 110277-64-0

DBGET integrated database retrieval system