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Literature summary extracted from

  • Jia, K.; Cao, R.; Hua, D.H.; Li, P.
    Study of class I and class III polyhydroxyalkanoate (PHA) synthases with substrates containing a modified side chain (2016), Biomacromolecules, 17, 1477-1485 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.3.1.304 bovine serum albumin addition of BSA increases the specific activity of enzyme PhaCCs with HBCoA about 2fold Chromobacterium sp. USM2
2.3.1.304 bovine serum albumin leads to an activity increase of severalfold when BSA is added to a concentration of 0.5 mg/mL (0.0075 mM) in the assay mixture Allochromatium vinosum
2.3.1.304 additional information molecular activation mechanism, overview Allochromatium vinosum
2.3.1.304 additional information molecular activation mechanism, overview Chromobacterium sp. USM2
2.3.1.304 additional information no significant activation of enzyme PhaCCc by bovine serum albumin, molecular activation mechanism, overview Caulobacter vibrioides

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.304 enzyme PhaCCc, recombinant expression Caulobacter vibrioides
2.3.1.304 enzyme PhaECAv, recombinant expression Allochromatium vinosum
2.3.1.304 gene phaC, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Chromobacterium sp. USM2

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.304 A479S site-directed mutagenesis, while mutant A479S-PhaCCs displays the same order as the wild-type enzyme with regard to chain length, it exhibits higher activity for both HBCoA and HVCoA and lower activity for HHxCoA compared to wild-type Chromobacterium sp. USM2

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.304 additional information no inhibition by bovine serum albumin Allochromatium vinosum
2.3.1.304 additional information no inhibition by bovine serum albumin Caulobacter vibrioides
2.3.1.304 additional information no inhibition by bovine serum albumin Chromobacterium sp. USM2

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.304 additional information
-
 additional information Michaelis-Menten kinetics Allochromatium vinosum
2.3.1.304 additional information
-
 additional information Michaelis-Menten kinetics Chromobacterium sp. USM2
2.3.1.304 additional information
-
 additional information Michaelis-Menten kinetics. Caulobacter crescentus class I PHA synthase uniquely lacks of a lag phase in its polymerization kinetics Caulobacter vibrioides
2.3.1.304 0.05
-
 3-(R)-hydroxhex-5-enoyl-CoA recombinant enzyme, pH 7.8, 30°C Allochromatium vinosum
2.3.1.304 0.05
-
 3-(R)-hydroxyhex5-ynoyl-CoA recombinant enzyme, pH 7.8, 30°C Allochromatium vinosum
2.3.1.304 0.07
-
 3-(S)-hydroxy-4-azidobutyryl-CoA recombinant enzyme, pH 7.8, 30°C Allochromatium vinosum
2.3.1.304 0.11
-
 (R)-3-hydroxyvaleryl-CoA recombinant enzyme, pH 7.8, 30°C Allochromatium vinosum
2.3.1.304 0.11
-
 (R)-3-hydroxybutanoyl-CoA recombinant enzyme, pH 7.8, 30°C Allochromatium vinosum
2.3.1.304 0.29
-
 (R)-3-hydroxybutanoyl-CoA recombinant enzyme, pH 7.8, 30°C Caulobacter vibrioides
2.3.1.304 1.54
-
 3-(R)-hydroxyhex5-ynoyl-CoA recombinant enzyme, pH 7.8, 30°C Caulobacter vibrioides
2.3.1.304 2.07
-
 (R)-3-hydroxyvaleryl-CoA recombinant enzyme, pH 7.8, 30°C Caulobacter vibrioides
2.3.1.304 3.22
-
 3-(R)-hydroxhex-5-enoyl-CoA recombinant enzyme, pH 7.8, 30°C Caulobacter vibrioides
2.3.1.304 9.46
-
 3-(S)-hydroxy-4-azidobutyryl-CoA recombinant enzyme, pH 7.8, 30°C Caulobacter vibrioides

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.304 (R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n Allochromatium vinosum
-
 [(R)-3-hydroxybutanoate](n+1) + CoA
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.304 Allochromatium vinosum
-
-
-
2.3.1.304 Caulobacter vibrioides A0A290N3S7
-
-
2.3.1.304 Chromobacterium sp. USM2 E1APK1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.304 recombinant enzyme PhaCCc Caulobacter vibrioides
2.3.1.304 recombinant enzyme PhaECAv Allochromatium vinosum
2.3.1.304 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration Chromobacterium sp. USM2

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.304 (R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n
-
 Allochromatium vinosum [(R)-3-hydroxybutanoate](n+1) + CoA
-
 ?
2.3.1.304 (R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n substrate HBCoA Allochromatium vinosum [(R)-3-hydroxybutanoate](n+1) + CoA
-
 ?
2.3.1.304 (R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n substrate HBCoA Chromobacterium sp. USM2 [(R)-3-hydroxybutanoate](n+1) + CoA
-
 ?
2.3.1.304 (R)-3-hydroxybutanoyl-CoA + [(R)-3-hydroxybutanoate]n substrate HBCoA Caulobacter vibrioides [(R)-3-hydroxybutanoate](n+1) + CoA
-
 ?
2.3.1.304 (R)-3-hydroxycapryl-CoA + [(R)-3-hydroxybutanoate]n substrate HCCoA Allochromatium vinosum ? + CoA
-
 ?
2.3.1.304 (R)-3-hydroxycapryl-CoA + [(R)-3-hydroxybutanoate]n substrate HCCoA Chromobacterium sp. USM2 ? + CoA
-
 ?
2.3.1.304 (R)-3-hydroxycapryl-CoA + [(R)-3-hydroxybutanoate]n substrate HCCoA Caulobacter vibrioides ? + CoA
-
 ?
2.3.1.304 (R)-3-hydroxyvaleryl-CoA + [(R)-3-hydroxybutanoate]n substrate HVCoA Allochromatium vinosum ? + CoA
-
 ?
2.3.1.304 (R)-3-hydroxyvaleryl-CoA + [(R)-3-hydroxybutanoate]n substrate HVCoA Chromobacterium sp. USM2 ? + CoA
-
 ?
2.3.1.304 (R)-3-hydroxyvaleryl-CoA + [(R)-3-hydroxybutanoate]n substrate HVCoA Caulobacter vibrioides ? + CoA
-
 ?
2.3.1.304 3-(R)-hydroxhex-5-enoyl-CoA + [(R)-3-hydroxybutanoate]n substrate HHxeCoA Allochromatium vinosum ? + CoA
-
 ?
2.3.1.304 3-(R)-hydroxhex-5-enoyl-CoA + [(R)-3-hydroxybutanoate]n substrate HHxeCoA Chromobacterium sp. USM2 ? + CoA
-
 ?
2.3.1.304 3-(R)-hydroxhex-5-enoyl-CoA + [(R)-3-hydroxybutanoate]n substrate HHxeCoA, low activity Caulobacter vibrioides ? + CoA
-
 ?
2.3.1.304 3-(R)-hydroxyhex5-ynoyl-CoA + [(R)-3-hydroxybutanoate]n substrate HHxyCoA Allochromatium vinosum ? + CoA
-
 ?
2.3.1.304 3-(R)-hydroxyhex5-ynoyl-CoA + [(R)-3-hydroxybutanoate]n substrate HHxyCoA Chromobacterium sp. USM2 ? + CoA
-
 ?
2.3.1.304 3-(R)-hydroxyhex5-ynoyl-CoA + [(R)-3-hydroxybutanoate]n substrate HHxyCoA, low activity Caulobacter vibrioides ? + CoA
-
 ?
2.3.1.304 3-(S)-hydroxy-4-azidobutyryl-CoA + [(R)-3-hydroxybutanoate]n substrate HABCoA Allochromatium vinosum ? + CoA
-
 ?
2.3.1.304 3-(S)-hydroxy-4-azidobutyryl-CoA + [(R)-3-hydroxybutanoate]n substrate HABCoA Chromobacterium sp. USM2 ? + CoA
-
 ?
2.3.1.304 3-(S)-hydroxy-4-azidobutyryl-CoA + [(R)-3-hydroxybutanoate]n substrate HABCoA, low activity Caulobacter vibrioides ? + CoA
-
 ?
2.3.1.304 additional information synthesis of a series of 3-(R)-hydroxyacyl CoA (HACoA) analogues as enzyme substrates, substrate specificity compared to class I PHA synthases, overview. The HHxyCoA and HABCoA can be efficiently incorporated into the polymers produced by enzyme PhaECAv. HHxCoA can be metabolically generated from 3-(R)-hydroxy-5-hexynoic acid. The activity of PhaECAv drops significantly with increasing length of the side chain in substrates. For example, the polymerization rates of HVCoA, HHxCoA, and HCCoA catalyzed by PhaECAv are measured at 23%, 0.38%, and 0.005% rate of HBCoA, respectively. No or poor activity with 3-(R)-hydroxy-4-phenylbutyryl-CoA (HPBCoA). Class III PhaECAv can polymerize HABCoA 6.5fold faster than HHxyCoA Allochromatium vinosum ?
-
-
2.3.1.304 additional information synthesis of a series of 3-(R)-hydroxyacyl CoA (HACoA) analogues as enzyme substrates, substrate specificity compared to class III PHA synthase, overview. PhaCCc displays 2.5fold lower activity with HABCoA than with HHxyCoA Caulobacter vibrioides ?
-
-
2.3.1.304 additional information synthesis of a series of 3-(R)-hydroxyacyl CoA (HACoA) analogues as enzyme substrates, substrate specificity compared to class III PHA synthase, overview. Priming of PhaCCc with saturated trimeric HBCoA (named sTCoA) demonstrates that approximately one equivalent CoA per PhaC is released during enzyme assay. This is quite different from other reported class I synthases. Wild-type PhaCCs has similar activities toward HHxyCoA and HABCoA Chromobacterium sp. USM2 ?
-
-

Synonyms

EC Number Synonyms Comment Organism
2.3.1.304 class I PHA synthase
-
 Chromobacterium sp. USM2
2.3.1.304 class I PHA synthase
-
 Caulobacter vibrioides
2.3.1.304 class I polyhydroxyalkanoate synthase
-
 Chromobacterium sp. USM2
2.3.1.304 class I polyhydroxyalkanoate synthase
-
 Caulobacter vibrioides
2.3.1.304 Class I synthase
-
 Chromobacterium sp. USM2
2.3.1.304 Class I synthase
-
 Caulobacter vibrioides
2.3.1.304 class III PHA synthase
-
 Allochromatium vinosum
2.3.1.304 class III polyhydroxyalkanoate synthase
-
 Allochromatium vinosum
2.3.1.304 class III synthase
-
 Allochromatium vinosum
2.3.1.304 PHA synthase
-
 Chromobacterium sp. USM2
2.3.1.304 PHA synthase
-
 Caulobacter vibrioides
2.3.1.304 PhaC
-
 Chromobacterium sp. USM2
2.3.1.304 PhaC
-
 Caulobacter vibrioides
2.3.1.304 PhaCCc
-
 Caulobacter vibrioides
2.3.1.304 PhaCCs
-
 Chromobacterium sp. USM2
2.3.1.304 PhaECAv
-
 Allochromatium vinosum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.304 30
-
 assay at Allochromatium vinosum
2.3.1.304 30
-
 assay at Chromobacterium sp. USM2
2.3.1.304 30
-
 assay at Caulobacter vibrioides

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.1.304 0.06
-
 3-(R)-hydroxhex-5-enoyl-CoA recombinant enzyme, pH 7.8, 30°C Caulobacter vibrioides
2.3.1.304 0.13
-
 3-(R)-hydroxyhex5-ynoyl-CoA recombinant enzyme, pH 7.8, 30°C Caulobacter vibrioides
2.3.1.304 0.19
-
 3-(S)-hydroxy-4-azidobutyryl-CoA recombinant enzyme, pH 7.8, 30°C Caulobacter vibrioides
2.3.1.304 2.99
-
 3-(R)-hydroxyhex5-ynoyl-CoA recombinant enzyme, pH 7.8, 30°C Allochromatium vinosum
2.3.1.304 12.7
-
 3-(R)-hydroxhex-5-enoyl-CoA recombinant enzyme, pH 7.8, 30°C Allochromatium vinosum
2.3.1.304 14.4
-
 (R)-3-hydroxyvaleryl-CoA recombinant enzyme, pH 7.8, 30°C Caulobacter vibrioides
2.3.1.304 20
-
 3-(S)-hydroxy-4-azidobutyryl-CoA recombinant enzyme, pH 7.8, 30°C Allochromatium vinosum
2.3.1.304 75
-
 (R)-3-hydroxybutanoyl-CoA recombinant enzyme, pH 7.8, 30°C Caulobacter vibrioides
2.3.1.304 98.1
-
 (R)-3-hydroxyvaleryl-CoA recombinant enzyme, pH 7.8, 30°C Allochromatium vinosum
2.3.1.304 508
-
 (R)-3-hydroxybutanoyl-CoA recombinant enzyme, pH 7.8, 30°C Allochromatium vinosum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.304 7.8
-
 assay at Allochromatium vinosum
2.3.1.304 7.8
-
 assay at Chromobacterium sp. USM2
2.3.1.304 7.8
-
 assay at Caulobacter vibrioides

General Information

EC Number General Information Comment Organism
2.3.1.304 physiological function different PHA synthases display distinct preference with regard to the length of the alkyl side chains, they can withstand moderate side chain modifications such as terminal unsaturated bonds and the azide group Allochromatium vinosum
2.3.1.304 physiological function different PHA synthases display distinct preference with regard to the length of the alkyl side chains, they can withstand moderate side chain modifications such as terminal unsaturated bonds and the azide group Caulobacter vibrioides
2.3.1.304 physiological function different PHA synthases display distinct preference with regard to the length of the alkyl side chains, they can withstand moderate side chain modifications such as terminal unsaturated bonds and the azide group. Specifically, the specific activity of PhaCCs toward propynyl analogue (HHxyCoA) is only 5fold less than that toward the classical substrate HBCoA Chromobacterium sp. USM2

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.3.1.304 0.019
-
 3-(R)-hydroxhex-5-enoyl-CoA recombinant enzyme, pH 7.8, 30°C Caulobacter vibrioides
2.3.1.304 0.02
-
 3-(S)-hydroxy-4-azidobutyryl-CoA recombinant enzyme, pH 7.8, 30°C Caulobacter vibrioides
2.3.1.304 0.084
-
 3-(R)-hydroxyhex5-ynoyl-CoA recombinant enzyme, pH 7.8, 30°C Caulobacter vibrioides
2.3.1.304 6.96
-
 (R)-3-hydroxyvaleryl-CoA recombinant enzyme, pH 7.8, 30°C Caulobacter vibrioides
2.3.1.304 59.8
-
 3-(R)-hydroxyhex5-ynoyl-CoA recombinant enzyme, pH 7.8, 30°C Allochromatium vinosum
2.3.1.304 254
-
 3-(R)-hydroxhex-5-enoyl-CoA recombinant enzyme, pH 7.8, 30°C Allochromatium vinosum
2.3.1.304 258.6
-
 (R)-3-hydroxybutanoyl-CoA recombinant enzyme, pH 7.8, 30°C Caulobacter vibrioides
2.3.1.304 285.7
-
 3-(S)-hydroxy-4-azidobutyryl-CoA recombinant enzyme, pH 7.8, 30°C Allochromatium vinosum
2.3.1.304 891.8
-
 (R)-3-hydroxyvaleryl-CoA recombinant enzyme, pH 7.8, 30°C Allochromatium vinosum
2.3.1.304 4618.2
-
 (R)-3-hydroxybutanoyl-CoA recombinant enzyme, pH 7.8, 30°C Allochromatium vinosum