EC 2.3.1.225
- Protein S-acyltransferase
IntEnz Enzyme Nomenclature
EC 2.3.1.225
Names
Accepted name:
protein S-acyltransferase
Other
names:
DHHC palmitoyl transferase
S-protein acyltransferase
G-protein palmitoyltransferase
Systematic name:
palmitoyl-CoA:[protein]-L-cysteine S-palmitoyltransferase
Reaction
-
hexadecanoyl-CoA
hexadecanoyl-CoA
Name origin:
UniProt - CHECKED (C)
Formula:
C37H62N7O17P3S
Charge: -4
ChEBI compound status: CHECKED (C)
+
L-cysteinyl-[protein]
L-cysteinyl-[protein]
GENERIC:10131
Is ROOT:
no
ROOT compound: GENERIC:9624
Number of residues: 1
L-cysteine residue
L-cysteine residue
Name origin:
UniProt - CHECKED (C)
Formula:
C3H5NOS
Charge: 0
Position: undefined
ChEBI compound status: CHECKED (C)
|
=
CoA
CoA
Name origin:
UniProt - CHECKED (C)
Formula:
C21H32N7O16P3S
Charge: -4
ChEBI compound status: CHECKED (C)
+
S-hexadecanoyl-L-cysteinyl-[protein]
S-hexadecanoyl-L-cysteinyl-[protein]
GENERIC:11032
Is ROOT:
no
ROOT compound: GENERIC:9624
Number of residues: 1
S-palmitoyl-L-cysteine residue
S-palmitoyl-L-cysteine residue
Name origin:
UniProt - CHECKED (C)
Formula:
C19H35NO2S
Charge: 0
Position: undefined
ChEBI compound status: CHECKED (C)
|
Comments:
The enzyme catalyses the posttranslational protein palmitoylation that plays a role in protein-membrane interactions, protein trafficking, and enzyme activity. Palmitoylation increases the hydrophobicity of proteins or protein domains and contributes to their membrane association.
Links to other databases
AKR1_ASHGO
AKR1_ASPFU
AKR1_ASPOR
AKR1_CANAL
AKR1_CANGA
AKR1_CRYNB
AKR1_CRYNJ
AKR1_DEBHA
AKR1_EMENI
AKR1_GIBZE
AKR1_KLULA
AKR1_LACK1
AKR1_MORAP
AKR1_NAUCC
AKR1_NEUCR
AKR1_SACU7
AKR1_SCHPO
AKR1_USTMA
AKR1_YARLI
AKR1_YEAST
AKR2_SACU7
AKR2_YEAST
APP-2_DROME
APP-3_DROME
APP-4_DROME
APP_DROME
DHC3A_DANRE
DHC5A_DANRE
DHC5B_DANRE
ERFB_ASHGO
ERFB_ASPFU
ERFB_CANAL
ERFB_CANGA
ERFB_DEBHA
ERFB_EMENI
ERFB_GIBZE
ERFB_KLULA
ERFB_NEUCR
ERFB_SCHPO
ERFB_YARLI
ERFB_YEAST
GLNA_ACOCA
GLNA_BOVIN
GLNA_CANLF
GLNA_CRIGR
GLNA_HUMAN
GLNA_MACFA
GLNA_MOUSE
GLNA_PIG
GLNA_RAT
HIP14_DROME
PFA3_ASHGO
PFA3_ASPFU
PFA3_CANAL
PFA3_CANGA
PFA3_DEBHA
PFA3_EMENI
PFA3_GIBZE
PFA3_KLULA
PFA3_NEUCR
PFA3_YARLI
PFA3_YEAST
PFA4-2_CRYNB
PFA4-2_CRYNJ
PFA4_ASHGO
PFA4_ASPFU
PFA4_CANAL
PFA4_CANGA
PFA4_CRYNB
PFA4_CRYNH
PFA4_CRYNJ
PFA4_DEBHA
PFA4_EMENI
PFA4_GIBZE
PFA4_KLULA
PFA4_NEUCR
PFA4_USTMA
PFA4_YARLI
PFA4_YEAST
PFA5_ASHGO
PFA5_ASPFU
PFA5_CANAL
PFA5_CANGA
PFA5_DEBHA
PFA5_EMENI
PFA5_GIBZE
PFA5_KLULA
PFA5_SCHPO
PFA5_YARLI
PFA5_YEAST
SWF1_ASHGO
SWF1_ASPFU
SWF1_CANAL
SWF1_CANGA
SWF1_DEBHA
SWF1_EMENI
SWF1_KLULA
SWF1_NEUCR
SWF1_SCHPO
SWF1_YARLI
SWF1_YEAST
ZD12A_DANRE
ZD12B_DANRE
ZD16A_DANRE
ZD16B-2_DANRE
ZD16B-3_DANRE
ZD16B-4_DANRE
ZD16B_DANRE
ZD18A_DANRE
ZD18B_DANRE
ZD20A_DANRE
ZD20B_DANRE
ZD23A_DANRE
ZD23B_DANRE
ZDH10_ARATH
ZDH11-2_HUMAN
ZDH11_ARATH
ZDH11_DANRE
ZDH11_HUMAN
ZDH11_MOUSE
ZDH12-2_HUMAN
ZDH12-2_MOUSE
ZDH12-3_HUMAN
ZDH12_ARATH
ZDH12_HUMAN
ZDH12_MOUSE
ZDH12_RAT
ZDH13-2_HUMAN
ZDH13-3_HUMAN
ZDH13_ARATH
ZDH13_HUMAN
ZDH13_MACFA
ZDH13_MOUSE
ZDH13_PONAB
ZDH14-2_HUMAN
ZDH14-2_MOUSE
ZDH14_ARATH
ZDH14_DANRE
ZDH14_HUMAN
ZDH14_MOUSE
ZDH15-2_HUMAN
ZDH15-3_HUMAN
ZDH15_ARATH
ZDH15_HUMAN
ZDH15_MOUSE
ZDH15_RAT
ZDH15_XENLA
ZDH16-2_BOVIN
ZDH16-2_HUMAN
ZDH16-3_HUMAN
ZDH16-4_HUMAN
ZDH16_ARATH
ZDH16_BOVIN
ZDH16_HUMAN
ZDH16_MACFA
ZDH16_MOUSE
ZDH17-2_HUMAN
ZDH17-2_MOUSE
ZDH17-3_HUMAN
ZDH17_ARATH
ZDH17_DANRE
ZDH17_HUMAN
ZDH17_MOUSE
ZDH17_RAT
ZDH18-2_HUMAN
ZDH18_ARATH
ZDH18_HUMAN
ZDH18_MOUSE
ZDH18_RAT
ZDH19-2_HUMAN
ZDH19-3_HUMAN
ZDH19_ARATH
ZDH19_HUMAN
ZDH19_MOUSE
ZDH20-2_HUMAN
ZDH20-2_MOUSE
ZDH20-3_HUMAN
ZDH20-4_HUMAN
ZDH20_ARATH
ZDH20_BOVIN
ZDH20_HUMAN
ZDH20_MOUSE
ZDH21_ARATH
ZDH21_BOVIN
ZDH21_DANRE
ZDH21_HUMAN
ZDH21_MOUSE
ZDH21_PONAB
ZDH22_ARATH
ZDH22_DANRE
ZDH22_HUMAN
ZDH22_MOUSE
ZDH22_RAT
ZDH23-2_RAT
ZDH23_ARATH
ZDH23_HUMAN
ZDH23_MOUSE
ZDH23_RAT
ZDH24-2_ARATH
ZDH24-3_ARATH
ZDH24_ARATH
ZDH24_DANRE
ZDH24_HUMAN
ZDH24_MOUSE
ZDH24_RAT
ZDH8B_DANRE
ZDHC1_ARATH
ZDHC1_DANRE
ZDHC1_DICDI
ZDHC1_HUMAN
ZDHC1_MOUSE
ZDHC2_ARATH
ZDHC2_DANRE
ZDHC2_DICDI
ZDHC2_HUMAN
ZDHC2_MOUSE
ZDHC2_RAT
ZDHC3-2_HUMAN
ZDHC3_ARATH
ZDHC3_DICDI
ZDHC3_HUMAN
ZDHC3_MOUSE
ZDHC3_RAT
ZDHC4_ARATH
ZDHC4_BOVIN
ZDHC4_DANRE
ZDHC4_DICDI
ZDHC4_HUMAN
ZDHC4_MOUSE
ZDHC4_RAT
ZDHC5-2_ARATH
ZDHC5-2_HUMAN
ZDHC5-2_MOUSE
ZDHC5_ARATH
ZDHC5_BOVIN
ZDHC5_CANLF
ZDHC5_DICDI
ZDHC5_HUMAN
ZDHC5_MOUSE
ZDHC5_PANTR
ZDHC5_PONAB
ZDHC5_RAT
ZDHC6-2_HUMAN
ZDHC6-2_MOUSE
ZDHC6-3_MOUSE
ZDHC6-4_MOUSE
ZDHC6_ARATH
ZDHC6_BOVIN
ZDHC6_DANRE
ZDHC6_DICDI
ZDHC6_HUMAN
ZDHC6_MOUSE
ZDHC6_PONAB
ZDHC7-2_HUMAN
ZDHC7_ARATH
ZDHC7_DANRE
ZDHC7_DICDI
ZDHC7_HUMAN
ZDHC7_MOUSE
ZDHC7_RAT
ZDHC8-2_HUMAN
ZDHC8-3_HUMAN
ZDHC8_ARATH
ZDHC8_CANLF
ZDHC8_DICDI
ZDHC8_HUMAN
ZDHC8_MOUSE
ZDHC8_PANTR
ZDHC9_ARATH
ZDHC9_BOVIN
ZDHC9_DANRE
ZDHC9_HUMAN
ZDHC9_MOUSE
ZDHC9_PONAB
ZDHCS_CAEEL
ZH11B_HUMAN
ZH15A_DANRE
ZH15B_DANRE
References
-
Dunphy, J. T., Greentree, W. K., Manahan, C. L., Linder, M. E.
G-protein palmitoyltransferase activity is enriched in plasma membranes.
J. Biol. Chem.
271
:
7154-7159
(1996).
[PMID:
8636152]
-
Veit, M., Dietrich, L. E., Ungermann, C.
Biochemical characterization of the vacuolar palmitoyl acyltransferase.
FEBS Lett.
540
:
101-105
(2003).
[PMID:
12681491]
-
Batistic, O.
Genomics and localization of the Arabidopsis DHHC-cysteine-rich domain S-acyltransferase protein family.
Plant Physiol.
160
:
1597-1612
(2012).
[PMID:
22968831]
-
Jennings, B. C., Linder, M. E.
DHHC protein S-acyltransferases use similar ping-pong kinetic mechanisms but display different acyl-CoA specificities.
J. Biol. Chem.
287
:
7236-7245
(2012).
[PMID:
22247542]
-
Zhou, L. Z., Li, S., Feng, Q. N., Zhang, Y. L., Zhao, X., Zeng, Y. L., Wang, H., Jiang, L., Zhang, Y.
Protein S-ACYL Transferase10 is critical for development and salt tolerance in Arabidopsis.
Plant Cell
25
:
1093-1107
(2013).
[PMID:
23482856]
[EC 2.3.1.225 created 2013]