KEGG   ENZYME: 3.5.1.92Help
Entry
EC 3.5.1.92                 Enzyme                                 

Name
pantetheine hydrolase;
pantetheinase;
vanin;
vanin-1
Class
Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amides
BRITE hierarchy
Sysname
(R)-pantetheine amidohydrolase
Reaction(IUBMB)
(R)-pantetheine + H2O = (R)-pantothenate + 2-aminoethanethiol [RN:R02973]
Reaction(KEGG)
Substrate
(R)-pantetheine [CPD:C00831];
H2O [CPD:C00001]
Product
(R)-pantothenate [CPD:C00864];
2-aminoethanethiol [CPD:C01678]
Comment
The enzyme hydrolyses only one of the amide bonds of pantetheine. The substrate analogues phosphopantetheine and CoA are not substrates. The enzyme recycles pantothenate (vitamin B5) and produces 2-aminoethanethiol (cysteamine), a potent anti-oxidant [5].
History
EC 3.5.1.92 created 2006
Pathway
ec00770  Pantothenate and CoA biosynthesis
Orthology
K08069  pantetheine hydrolase
Genes
HSA: 55350(VNN3) 8875(VNN2) 8876(VNN1)
PTR: 463006(VNN3) 463007(VNN2) 746544(VNN1)
PPS: 100978332(VNN1) 100978987(VNN3) 100979321(VNN2)
GGO: 101125335(VNN1) 101126064(VNN3) 101126426(VNN2)
PON: 100436777 100441056(VNN1) 100441798(VNN3)
NLE: 100579766(VNN1) 100580443
MCC: 708637(VNN2) 708748(VNN3) 708830(VNN1)
MCF: 101865481 102139623(VNN1) 102139985
CSAB: 103240351(VNN2) 103240352 103240354
RRO: 104657993(VNN2) 104657995 104657997(VNN1)
CJC: 100399050(VNN1) 100399411 100895783(VNN2)
SBQ: 101042912 101043241(VNN1)
MMU: 22361(Vnn1) 26464(Vnn3)
RNO: 29142(Vnn1) 498992(Vnn3)
CGE: 100750608(Vnn1) 100754161
NGI: 103724951(Vnn2) 103724954(Vnn1)
HGL: 101710059(Vnn1) 101724572(Vnn3)
CCAN: 109687501(Vnn3) 109687502(Vnn1) 109687517(Vnn2)
OCU: 100344919 100345689(VNN2) 100356303(VNN1)
TUP: 102490124(VNN1) 102490829(VNN3) 102491237(VNN2)
CFA: 442973(VNN1)
AML: 100465598(VNN1)
UMR: 103663395(VNN1) 103663501
ORO: 101376044(VNN1) 101385601(VNN3) 105757466(VNN2)
PTG: 102970509(VNN3) 102971182(VNN1)
AJU: 106976871 106976873(VNN1)
BTA: 526704(VNN1) 534929(VNN2) 785817(VNN3)
BOM: 102269407(VNN1) 102269960(VNN2)
BIU: 109563954(VNN1) 109563957
PHD: 102330000(VNN1) 102330608(VNN2) 102338197
CHX: 102172899(VNN1) 102173569(VNN2)
OAS: 101105005(VNN1) 101105417(VNN2)
SSC: 100152784(VNN3) 100153984(VNN2) 397246(VNN1)
CFR: 102514326(VNN1) 102514743 102515010(VNN2)
CDK: 105096352(VNN1) 105096353 105096354(VNN2)
BACU: 103010543(VNN1) 103011016 103011299(VNN2)
LVE: 103079030(VNN2) 103079497(VNN1) 103084601
OOR: 101284042(VNN2) 101284462(VNN1) 101286152(VNN3)
EPZ: 103557081(VNN2) 103557083 103557085(VNN1)
MYB: 102246494(VNN1) 102247599 102247887(VNN2)
MYD: 102761007(VNN1) 102761476(VNN2) 102772945
PALE: 102881910(VNN3) 102882154(VNN1) 102894153(VNN2)
LAV: 100670289 100671136(VNN1)
MDO: 100031271(VNN1) 100031277(VNN3)
OAA: 100074927(VNN1) 100074964 100075001(VNN2)
GGA: 421702(VNN1)
TGU: 100217969(VNN1) 100220807 100223749(VNN2)
GFR: 102038583(VNN1) 102041126(VNN2)
PMAJ: 107201269(VNN3) 107202003
FPG: 101924145(VNN3) 101924317
PSS: 102445936(VNN1) 102446172(VNN3)
CMY: 102942174
CPIC: 101932537 101933999(VNN1)
PVT: 110071965 110071970(VNN1)
GJA: 107110525(VNN1) 107110527
XTR: 496642(vnn1) 496713(vnn2)
NPR: 108799348
SPU: 575770
APLC: 110985242
SKO: 100371918
MDE: 101892216
HST: 105187950
DPA: 109537053
PMAC: 106709937
PXY: 105389407
FCD: 110862115
TUT: 107372229
CRG: 105345878
EPA: 110253943
ADF: 107357429
DFA: DFA_09026
SMIN: v1.2.032492.t1(symbB.v1.2.032492.t1) v1.2.033951.t1(symbB.v1.2.033951.t1)
NGR: NAEGRDRAFT_78567(AM31)
 » show all
Taxonomy
Reference
1  [PMID:440106]
  Authors
Dupre S, Cavallini D.
  Title
Purification and properties of pantetheinase from horse kidney.
  Journal
Methods. Enzymol. 62 (1979) 262-7.
Reference
2  [PMID:6549111]
  Authors
Dupre S, Chiaraluce R, Nardini M, Cannella C, Ricci G, Cavallini D.
  Title
Continuous spectrophotometric assay of pantetheinase activity.
  Journal
Anal. Biochem. 142 (1984) 175-81.
Reference
3  [PMID:10567687]
  Authors
Maras B, Barra D, Dupre S, Pitari G.
  Title
Is pantetheinase the actual identity of mouse and human vanin-1 proteins?
  Journal
FEBS. Lett. 461 (1999) 149-52.
  Sequence
[hsa:8876] [mmu:22361]
Reference
4  [PMID:8934567]
  Authors
Aurrand-Lions M, Galland F, Bazin H, Zakharyev VM, Imhof BA, Naquet P.
  Title
Vanin-1, a novel GPI-linked perivascular molecule involved in thymus homing.
  Journal
Immunity. 5 (1996) 391-405.
  Sequence
[mmu:22361]
Reference
5  [PMID:11042271]
  Authors
Pitari G, Malergue F, Martin F, Philippe JM, Massucci MT, Chabret C, Maras B, Dupre S, Naquet P, Galland F.
  Title
Pantetheinase activity of membrane-bound Vanin-1: lack of free cysteamine in tissues of Vanin-1 deficient mice.
  Journal
FEBS. Lett. 483 (2000) 149-54.
  Sequence
[mmu:22361]
Reference
6  [PMID:11491533]
  Authors
Martin F, Malergue F, Pitari G, Philippe JM, Philips S, Chabret C, Granjeaud S, Mattei MG, Mungall AJ, Naquet P, Galland F.
  Title
Vanin genes are clustered (human 6q22-24 and mouse 10A2B1) and encode isoforms of pantetheinase ectoenzymes.
  Journal
Immunogenetics. 53 (2001) 296-306.
  Sequence
[hsa:8876 8875] [mmu:26464]
Reference
7  [PMID:11380987]
  Authors
Pace HC, Brenner C.
  Title
The nitrilase superfamily: classification, structure and function.
  Journal
Genome. Biol. 2 (2001) REVIEWS0001.
Other DBs
ExplorEnz - The Enzyme Database: 3.5.1.92
IUBMB Enzyme Nomenclature: 3.5.1.92
ExPASy - ENZYME nomenclature database: 3.5.1.92
BRENDA, the Enzyme Database: 3.5.1.92
CAS: 56093-18-6

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