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(3R)-3-hydroxy-hexanoyl-[acyl-carrier protein]
trans-2-hexenoyl-[acyl-carrier protein] + H2O
Substrates: Scalindua brodae apo-amxACP serves as acyl-carrier protein. The (3S)-epimer is not a substrate
Products: -
?
(3R)-3-hydroxybutyryl-[acyl-carrier protein]
2-butenoyl-[acyl-carrier protein] + H2O
Substrates: -
Products: -
?
(3R)-3-hydroxydecanoyl-[acyl-carrier protein]
2-decenoyl-[acyl-carrier protein] + H2O
(3R)-3-hydroxydecanoyl-[acyl-carrier protein]
trans-2-decenoyl-[acyl-carrier protein] + H2O
Substrates: -
Products: -
?
(3R)-3-hydroxydodecanoyl-[acyl-carrier protein]
2-dodecenoyl-[acyl-carrier protein] + H2O
-
Substrates: -
Products: -
?
(3R)-3-hydroxyheptanoyl-[acyl-carrier protein]
2-heptenoyl-[acyl-carrier protein] + H2O
-
Substrates: -
Products: -
?
(3R)-3-hydroxyhexanoyl-[acyl-carrier protein]
2-hexenoyl-[acyl-carrier protein] + H2O
-
Substrates: -
Products: -
?
(3R)-3-hydroxynonanoyl-[acyl-carrier protein]
2-nonenoyl-[acyl-carrier protein] + H2O
-
Substrates: -
Products: -
?
(3R)-3-hydroxyoctanoyl-[acyl-carrier protein]
2-octenoyl-[acyl-carrier protein] + H2O
-
Substrates: beta-hydroxyoctanoyl-ACP
Products: -
?
(3R)-3-hydroxyoctanoyl-[acyl-carrier protein]
trans-2-octenoyl-[acyl-carrier protein] + H2O
Substrates: -
Products: -
?
(3R)-3-hydroxyundecanoyl-[acyl-carrier protein]
2-undecenoyl-[acyl-carrier protein] + H2O
-
Substrates: -
Products: -
?
3-hydroxydecanoyl-N-acetylcysteamine
? + H2O
3-hydroxyhexanoyl-N-acetylcysteamine
? + H2O
3-hydroxyoctanoyl-N-acetylcysteamine
? + H2O
5-methyl-3-hydroxyhexanoyl-N-acetylcysteamine
? + H2O
6-methyl-3-hydroxyheptanoyl-N-acetylcysteamine
? + H2O
7-methyl-3-hydroxyoctanoyl-N-acetylcysteamine
? + H2O
Q9L0M4; Q9L0M3
Substrates: the N-acetylcysteamine group is structurally similar to the substrate binding end of the pantethine arm of acyl carrier proteins
Products: -
?
additional information
?
-
(3R)-3-hydroxydecanoyl-[acyl-carrier protein]

2-decenoyl-[acyl-carrier protein] + H2O
-
Substrates: -
Products: -
?
(3R)-3-hydroxydecanoyl-[acyl-carrier protein]
2-decenoyl-[acyl-carrier protein] + H2O
Substrates: -
Products: -
?
3-hydroxydecanoyl-N-acetylcysteamine

? + H2O
Q9L0M4; Q9L0M3
Substrates: the N-acetylcysteamine group is structurally similar to the substrate binding end of the pantethine arm of acyl carrier proteins
Products: -
?
3-hydroxydecanoyl-N-acetylcysteamine
? + H2O
Q9L0M4; Q9L0M3
Substrates: the N-acetylcysteamine group is structurally similar to the substrate binding end of the pantethine arm of acyl carrier proteins
Products: -
?
3-hydroxyhexanoyl-N-acetylcysteamine

? + H2O
Q9L0M4; Q9L0M3
Substrates: the N-acetylcysteamine group is structurally similar to the substrate binding end of the pantethine arm of acyl carrier proteins
Products: -
?
3-hydroxyhexanoyl-N-acetylcysteamine
? + H2O
Q9L0M4; Q9L0M3
Substrates: the N-acetylcysteamine group is structurally similar to the substrate binding end of the pantethine arm of acyl carrier proteins
Products: -
?
3-hydroxyoctanoyl-N-acetylcysteamine

? + H2O
Q9L0M4; Q9L0M3
Substrates: the N-acetylcysteamine group is structurally similar to the substrate binding end of the pantethine arm of acyl carrier proteins
Products: -
?
3-hydroxyoctanoyl-N-acetylcysteamine
? + H2O
Q9L0M4; Q9L0M3
Substrates: the N-acetylcysteamine group is structurally similar to the substrate binding end of the pantethine arm of acyl carrier proteins
Products: -
?
5-methyl-3-hydroxyhexanoyl-N-acetylcysteamine

? + H2O
Q9L0M4; Q9L0M3
Substrates: the N-acetylcysteamine group is structurally similar to the substrate binding end of the pantethine arm of acyl carrier proteins
Products: -
?
5-methyl-3-hydroxyhexanoyl-N-acetylcysteamine
? + H2O
Q9L0M4; Q9L0M3
Substrates: the N-acetylcysteamine group is structurally similar to the substrate binding end of the pantethine arm of acyl carrier proteins
Products: -
?
6-methyl-3-hydroxyheptanoyl-N-acetylcysteamine

? + H2O
Q9L0M4; Q9L0M3
Substrates: the N-acetylcysteamine group is structurally similar to the substrate binding end of the pantethine arm of acyl carrier proteins
Products: -
?
6-methyl-3-hydroxyheptanoyl-N-acetylcysteamine
? + H2O
Q9L0M4; Q9L0M3
Substrates: the N-acetylcysteamine group is structurally similar to the substrate binding end of the pantethine arm of acyl carrier proteins
Products: -
?
additional information

?
-
Substrates: amxFabZ efficiently converts substrates with acyl chain lengths of up to eight carbons, whereas longer substrates are converted much more slowly. amxFabZ does dehydrate substrates bound to amxACP, it does not convert substrates bound to canonical ACP of the same organism
Products: -
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additional information
?
-
-
Substrates: no activity on C14- or C16-ACP derivatives
Products: -
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additional information
?
-
-
Substrates: specific for 3-hydroxyacyl-[acyl-carrier protein] derivatives, C6 to C12, highest activity on C8 derivative
Products: -
?
additional information
?
-
-
Substrates: 3-Hydroxyacyl-[acyl-carrier protein] derivatives, C6 to C12
Products: -
?
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metabolism

important enzyme in controlling fatty acid chain length and saturation levels
metabolism
Q9L0M4; Q9L0M3
the enzyme also processes intermediates in both fatty acid and undecylprodiginine biosynthetic processes. It is capable of utilizing various chain lengths of straight- and branched-chain 3-hydroxyacyl-N-acetyl cysteamine substrates. FabA does not discriminate between acyl carrier proteins from primary and secondary metabolism. It processes intermediates for both biosynthetic pathways
metabolism
the enzyme catalyzes the third of the four iterative reactions that constitute the mitochondrial fatty acid synthase cycle
metabolism
beta-hydroxyacyl-[acyl carrier protein (ACP)]-dehydratase is a component of the type II fatty acid synthase complex involved in de novo fatty acid biosynthesis in plants. Expression levels of HaHAD1 remains constant across most tissues suggest a housekeeping function
metabolism
beta-hydroxyacyl-[acyl carrier protein (ACP)]-dehydratase is a component of the type II fatty acid synthase complex involved in de novo fatty acid biosynthesis in plants. Higher levels of HaHAD2 in the initial stages of seed development inferr its key role in seed storage fatty acid synthesis
metabolism
-
the enzyme also processes intermediates in both fatty acid and undecylprodiginine biosynthetic processes. It is capable of utilizing various chain lengths of straight- and branched-chain 3-hydroxyacyl-N-acetyl cysteamine substrates. FabA does not discriminate between acyl carrier proteins from primary and secondary metabolism. It processes intermediates for both biosynthetic pathways
-
physiological function

-
in a missense mutant with significantly reduced enzymatic activity, some genes related to cell membrane constituents are downregulated in the mutant and the total fatty acid content in the mutant is significantly decreased relative to the wild type
physiological function
FabZ contributes to the growth and virulence of Toxoplasma gondii. In a FabZ deficient strain the apicoplast is partly lost and the growth ability of the parasite in vitro is significantly inhibited. The FabZ deficient strain exhibits reduced virulence for mice. Deletion of FabZ in the PRU significantly decreases the brain cyst burden in mice
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Mizugaki, M.; Swindell, A.C.; Wakil, S.J.
Intermediate- and long-chain beta-hydroxyacyl-ACP dehydratases from E. coli fatty acid synthetase
Biochem. Biophys. Res. Commun.
33
520-527
1968
Escherichia coli
brenda
Nguyen, C.; Haushalter, R.; Lee, D.; Markwick, P.; Bruegger, J.; Caldara-Festin, G.; Finzel, K.; Jackson, D.; Ishikawa, F.; O'Dowd, B.; McCammon, J.; Opella, S.; Tsai, S.; Burkart, M.
Trapping the dynamic acyl carrier protein in fatty acid biosynthesis
Nature
505
427-431
2014
Escherichia coli (P0A6Q3), Escherichia coli
brenda
Finzel, K.; Nguyen, C.; Jackson, D.R.; Gupta, A.; Tsai, S.C.; Burkart, M.D.
Probing the substrate specificity and protein-protein interactions of the E. coli fatty acid dehydratase, FabA
Chem. Biol.
22
1453-1460
2015
Escherichia coli (P0A6Q3), Escherichia coli
brenda
Singh, R.; Reynolds, K.A.
Identification and characterization of FabA from the type II fatty acid synthase of Streptomyces coelicolor
J. Nat. Prod.
79
240-243
2016
Streptomyces coelicolor (Q9L0M4 AND Q9L0M3), Streptomyces coelicolor, Streptomyces coelicolor ATCC BAA-471 (Q9L0M4 AND Q9L0M3)
brenda
Guan, X.; Okazaki, Y.; Lithio, A.; Li, L.; Zhao, X.; Jin, H.; Nettleton, D.; Saito, K.; Nikolau, B.J.
Discovery and characterization of the 3-hydroxyacyl-ACP dehydratase component of the plant mitochondrial fatty acid synthase system
Plant Physiol.
173
2010-2028
2017
Arabidopsis thaliana (Q9FJI2)
brenda
Gonzalez-Thuillier, I.; Venegas-Caleron, M.; Sanchez, R.; Garces, R.; von Wettstein-Knowles, P.; Martinez-Force, E.
Sunflower (Helianthus annuus) fatty acid synthase complex beta-hydroxyacyl-[acyl carrier protein] dehydratase genes
Planta
243
397-410
2016
Helianthus annuus (F2VYC9)
brenda
Xu, X.P.; Elsheikha, H.M.; Liu, W.G.; Zhang, Z.W.; Sun, L.X.; Liang, Q.L.; Song, M.X.; Zhu, X.Q.
The role of type II fatty acid synthesis enzymes FabZ, ODSCI, and ODSCII in the pathogenesis of Toxoplasma gondii infection
Front. Microbiol.
12
703059
2021
Toxoplasma gondii (O97376)
brenda
Liu, Z.; Wang, Z.; Gu, H.; You, J.; Hu, M.; Zhang, Y.; Zhu, Z.; Wang, Y.; Liu, S.; Chen, L.; Liu, X.; Tian, Y.; Zhou, S.; Jiang, L.; Liu, L.; Wan, J.
Identification and phenotypic characterization of ZEBRA LEAF16 encoding a beta-hydroxyacyl-ACP dehydratase in rice
Front. Plant Sci.
9
782
2018
Oryza sativa Indica Group
brenda
Dietl, A.; Wellach, K.; Mahadevan, P.; Mertes, N.; Winter, S.; Kutsch, T.; Walz, C.; Schlichting, I.; Fabritz, S.; Barends, T.M.
Structures of an unusual 3-hydroxyacyl dehydratase (FabZ) from a ladderane-producing organism with an unexpected substrate preference
J. Biol. Chem.
299
104602
2023
Candidatus Scalindua brodae (A0A0B0EHL2)
brenda