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onsdag 17 juli 2019

ihmisen sytosolisesta AcetylCoa syntetaasista ACSS2 (20q11.22)

 (Mainitsen että aiemmin sain eräästä lähteestä tietää, että vain sirtuiini SIRT1 pystyy deasetyloimaan tätä sytosolista asetyyliCoA-syntaasia, kun taas mitokondriaalista deasetyloi SIRT3. )


 ACSS2 ( 20q11.22), sytosolinen asetyyliCoA syntetaasi, etikkahapon aktivoija.
https://www.ncbi.nlm.nih.gov/gene/55902
Tämä geeni koodaa sytosolista etnsyymiä, joka  katalysoi etikkahapon aktivoitumista   ja  tämä aktivoitunut etikkahappo  voi käyttyä lipidisynteesiin tai energian generoimiseen. Proteiini toimii monomeerina ja  tuottaa asetyyli-CoA:n etikkahaposta reaktiossa, joka vaatii ATP:tä.
 Tämän geenin ilmentymää säätelee SREB- proteiinit, transkriptiotekijät, jotka aktivoivat geenejä, mitä vaaditaan  kolesterolin ja tyydyttymättömien rasvahappojen synteesin. Vaihtoehtoispleissauksista tulee useita  transkriptivariantteja. Geeniä ilmentyy laajasti rasvakudoksessa, pohjukaissuolesas ja 24 muussa kudoksessa. 
Official Symbol ACSS2
Official Full Name acyl-CoA synthetase short chain family member 2
Also known as ACS; ACSA; ACAS2; ACECS; dJ1161H23.1
Summary: This gene encodes a cytosolic enzyme that catalyzes the activation of acetate for use in lipid synthesis and energy generation. The protein acts as a monomer and produces acetyl-CoA from acetate in a reaction that requires ATP.
 Expression of this gene is regulated by sterol regulatory element-binding proteins, transcription factors that activate genes required for the synthesis of cholesterol and unsaturated fatty acids. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2009]
Expression: Broad expression in fat (RPKM 49.2), duodenum (RPKM 47.1) and 24 other tissues See more. Orthologs. mouse all.
Preferred Names
acetyl-coenzyme A synthetase, cytoplasmic

Names
acetate thiokinase
acetate-CoA ligase
acetyl-Coenzyme A synthetase 2 (ADP forming)
acyl-activating enzyme
cytoplasmic acetyl-coenzyme A synthetase
 
( Millä tavalla sytosolinen ja mitokondriaalinen ACSS eroavat  toisistaan rakenteellisesti? Mm. vaikuttaa olevan kuusi seriinifosforylaatiota ja vain yksi N-lysiiniasetylaatio tässä sytosolisessa. Tämä geeni sijaitsee saman kromosomin q päädyssä, kun mitokondrinen  ACSS taas sijaitsee p-päädyssä).
  
Features
NM_001076552.2NP_001070020.2  acetyl-coenzyme A synthetase, cytoplasmic isoform 2
 
FEATURES             Location/Qualifiers
     source          1..714
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.22"
     Protein         1..714
                     /product="acetyl-coenzyme A synthetase, cytoplasmic
                     isoform 2"
                     /EC_number="6.2.1.1"
                     /note="acetyl-Coenzyme A synthetase 2 (ADP forming);
                     cytoplasmic acetyl-coenzyme A synthetase; acetate-CoA
                     ligase; acyl-activating enzyme; acetate thiokinase;
                     acetyl-coenzyme A synthetase, cytoplasmic"
                     /calculated_mol_wt=79957
     Site            28
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine. {ECO:0000244|PubMed:23186163,
                     ECO:0000244|PubMed:24275569}; propagated from
                     UniProtKB/Swiss-Prot (Q9NR19.1)"
     Site            30
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine. {ECO:0000244|PubMed:18669648,
                     ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569};
                     propagated from UniProtKB/Swiss-Prot (Q9NR19.1)"
     Region          31..705
                     /region_name="PRK00174"
                     /note="acetyl-CoA synthetase; Provisional"
                     /db_xref="CDD:234677"
     Site            36
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine. {ECO:0000244|PubMed:24275569};
                     propagated from UniProtKB/Swiss-Prot (Q9NR19.1)"
     Region          51..698
                     /region_name="ACS"
                     /note="Acetyl-CoA synthetase (also known as acetate-CoA
                     ligase and acetyl-activating enzyme); cd05966"
                     /db_xref="CDD:213313"
     Site            order(191..193,219,222,224,370,375..376,398..400,424..425,
                     428,451..454,476..481,565,577,580,588..591,649,654..655)
                     /site_type="active"
                     /db_xref="CDD:213313"
     Site            order(191..193,219,222,224,370,376,398..400,424..425,428,
                     588..590,649,654)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:213313"
     Region          219..222
                     /region_name="Coenzyme A binding. {ECO:0000250}"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR19.1)"
     Site            263
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine. {ECO:0000250|UniProtKB:Q9QXG4};
                     propagated from UniProtKB/Swiss-Prot (Q9NR19.1)"
     Site            265
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine. {ECO:0000250|UniProtKB:Q9QXG4};
                     propagated from UniProtKB/Swiss-Prot (Q9NR19.1)"
     Site            267
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine. {ECO:0000244|PubMed:18669648,
                     ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163,
                     ECO:0000244|PubMed:24275569}; propagated from
                     UniProtKB/Swiss-Prot (Q9NR19.1)"
     Site            order(326,329..334,336..337)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:213313"
     Site            order(375..376,451..454,476..481,565,577,580,591)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:213313"
     Site            order(375..376,451..452,479)
                     /site_type="other"
                     /note="acetate binding site [chemical binding]"
                     /db_xref="CDD:213313"
     Site            431
                     /site_type="acetylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N6-acetyllysine. {ECO:0000244|PubMed:19608861};
                     propagated from UniProtKB/Swiss-Prot (Q9NR19.1)"
     CDS             1..714
                     /gene="ACSS2"
                     /gene_synonym="ACAS2; ACECS; ACS; ACSA; dJ1161H23.1"
                     /coded_by="NM_001076552.2:122..2266"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS42868.2"
                     /db_xref="GeneID:55902"
                     /db_xref="HGNC:HGNC:15814"
                     /db_xref="MIM:605832"
ORIGIN      
        1 mglpeervrs gsgsrgqeea gaggrarsws pppevsrsah vpslqryrel hrrsveepre
       61 fwgdiakefy wktpcpgpfl rynfdvtkgk ifiewmkgat tnicynvldr nvhekklgdk
      121 vafywegnep gettqityhq llvqvcqfsn vlrkqgiqkg drvaiympmi pelvvamlac
      181 arigalhsiv fagfsseslc erildsscsl littdafyrg eklvnlkela dealqkcqek
      241 gfpvrccivv khlgraelgm gdstsqsppi krscpdvqgk lkekskrvqp qiswnqgidl
      301 wwhelmqeag decepewcda edplfilyts gstgkpkgvv htvggymlyv attfkyvfdf
      361 haedvfwcta digwitghsy vtygplanga tsvlfegipt ypdvnrlwsi vdkykvtkfy
      421 taptairllm Kfgdepvtkh sraslqvlgt vgepinpeaw lwyhrvvgaq rcpivdtfwq
      481 tetgghmltp lpgatpmkpg satfpffgva pailnesgee legeaegylv fkqpwpgimr
      541 tvygnherfe ttyfkkfpgy yvtgdgcqrd qdgyywitgr iddmlnvsgh llstaevesa
      601 lveheavaea avvghphpvk geclycfvtl cdghtfspkl teelkkqire kigpiatpdy
      661 iqnapglpkt rsgkimrrvl rkiaqndhdl gdmstvadps vishlfshrc ltiq
//
(Mitä tietoja on tästä proteiinista saatu tähän mennessä?)
 
GeneRIFs: Gene References Into Functions
Submit: New GeneRIF Correction See all GeneRIFs (21)

https://www.ncbi.nlm.nih.gov/pubmed/?term=ACSS2%2C+Sirtuins 
https://www.ncbi.nlm.nih.gov/pubmed/?term=ACSS2%2C++hypercholesterolemia 
(Joku toinenkin on kiinnittänyt huomion ACSS- geenien  sijaintiin ja ominaisuuksiin ja  ei koodaavan pitkän RNA:n mahdolliseen  osuuteen. Otan aivan  tuoreen artikkelin pohdittavaksi. ACSS1 ja ACSS2  pitävät lyhyistä ja keskipitkistä rasvahapoista C2-C5  ensisijaisena kohteena C2 etikkahappoa.)  
https://www.ncbi.nlm.nih.gov/pubmed/31281828 
2019 Jun 2;2019:5070975. doi: 10.1155/2019/5070975. eCollection 2019.
Identification of lncRNAs and Genes Responsible for Fatness and Fatty Acid Composition Traits between the Tibetan and Yorkshire Pigs.
Shang P1, Li W2, Liu G3, Zhang J1, Li M1, Wu L1, Wang K2, Chamba Y1.

Abstract

Tibetan pigs from the Tibetan Plateau are characterized with a significant phenotypic difference relative to lowland pigs. In this study, a significant difference of the fatness and fatty acid composition traits was observed between the Tibetan and Yorkshire pigs. To uncover the involved mechanism, the expression profile of long noncoding RNAs (lncRNAs) and genes was compared between them. After serial filtered steps, 1,964 lncRNAs were obtained through our computational pipeline. In total, 63 and 715 lncRNAs and genes were identified to be differentially expressed. Evidence from cis- and trans-targeting analysis of lncRNAs demonstrated that some lncRNAs, such as MSTRG.14097 and MSTRG.8034, played important roles in the fatness and fatty acid composition traits. Bioinformatics analysis revealed that many candidate genes were responsible for the two traits. Of these, FASN, ACACA, SCD, ME3, PDHB, ACSS1, ACSS2, and ACLY were identified, which functioned in regulating the level of hexadecanoic acid, hexadecenoic acid, octadecenoic acid, and monounsaturated fatty acid. And LPGAT1, PDK4, ACAA1, and ADIPOQ were associated with the content of stearic acid, octadecadienoic acid, and polyunsaturated fatty acid. Candidate genes, which were responsible for fatness trait, consisted of FGF2, PLAG1, ADIPOQ, IRX3, MIF, IL-34, ADAM8, HMOX1, Vav1, and TLR8. In addition, association analysis also revealed that 34 and 57 genes significantly correlated to the fatness and fatty acid composition trait, respectively. Working out the mechanism caused by these lncRNAs and candidate genes is proven to be complicated but is invaluable to our understanding of fatness and fatty acid composition traits.


Aktivoidusta etikkahaposta ihmisen solussa ja mitokondriassa. Mitokondriaalinen ACSS1( 20p11.21)

AceSC1 ja AceC2
https://www.ncbi.nlm.nih.gov/pubmed/11150295
Näillä on nykyisin toiset  nimetm joissa numero on päinvastoin siis  ACSS2 sytosolinen  (AceCS1 ennen) ja  ACSS1 mitokondriaalinen ( AceCS2 ennen). Mitokondriaalista on eniten sydämessä ja maksasta se puuttuu.

AseCS1 on mitokondriaalinen asetyyli-CoA-syntetaasi. (Asetaatti-CoA ligaasi;  etikkahapon CoA-ligaasi) ,  Sillä on ainakin hiirissä - (joilla ei liikuntafaktoristaole puutetta)    tärkeä osuus sitruunahapposyklissä (CSC, TCA) , jossa se katalysoi asetaatit eli etikkahapon konversiota aktiiviksi etikkahapoksi , asetyyli CoA:ksi.( AsetyyliCoA taas on se perustava molekyyli, jolla on heti käyttöä monenmoisiin  metabolisiin teihin! Pelkkä etikkahappo taas tuottaa  harmia, jos se ei  kykene aktivoitumaan).  Geenistä pleissautuu  vaihtoehtoisia transkriptejä, jotka koodaavat  monia isoformeja. Tätä geeniä ilmentyy istukassa, pohjukaisisuolessa ja 24 muussa kudoksessa.
Geenin virallinen symboli nykyään on ACSS1, muita nimiä ovat ACAS2L, ACECS1, AceCS2L

ACSS1 (20p11.21) . acyl-CoA synthetase short chain family member 1 [ Homo sapiens (human) ]
https://www.ncbi.nlm.nih.gov/gene/84532
Official Symbol ACSS1
Official Full Name acyl-CoA synthetase short chain family member 1
Also known as ACAS2L; ACECS1; AceCS2L
Summary:  This gene encodes a mitochondrial acetyl-CoA synthetase enzyme. A similar protein in mice plays an important role in the tricarboxylic acid cycle by catalyzing the conversion of acetate to acetyl CoA. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Nov 2011]
Expression Broad expression in placenta (RPKM 70.4), duodenum (RPKM 23.0) and 24 other tissues See more Orthologs mouse all
Preferred Names: acetyl-coenzyme A synthetase 2-like, mitochondrial
Names: acetate--CoA ligase 2
Features: NM_001252675.1NP_001239604.1  acetyl-coenzyme A synthetase 2-like, mitochondrial isoform 2 precursor   ( Plenty of  isoforms!)
 
 
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p11.21"
     Protein         1..687
                     /product="acetyl-coenzyme A synthetase 2-like,
                     mitochondrial isoform 2 precursor"
                     /EC_number="6.2.1.1"
                     /note="acetyl-coenzyme A synthetase 2-like, mitochondrial;
                     acetate--CoA ligase 2"
                     /calculated_mol_wt=70901
     transit_peptide 1..37
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Mitochondrion. {ECO:0000269|PubMed:16788062};
                     propagated from UniProtKB/Swiss-Prot (Q9NUB1.2)"
                     /calculated_mol_wt=3743
     Region          54..674
                     /region_name="Ac_CoA_lig_AcsA"
                     /note="acetate--CoA ligase; TIGR02188"
                     /db_xref="CDD:274022"
     Region          64..665
                     /region_name="ACS"
                     /note="Acetyl-CoA synthetase (also known as acetate-CoA
                     ligase and acetyl-activating enzyme); cd05966"
                     /db_xref="CDD:213313"
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme)
Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Site order(196..198,224,227,229,335,340..341,363..365,389..390, 393,416..419,441..446,531,543,546,554..557,615,620..621) /site_type="active" /db_xref="CDD:213313" Site order(196..198,224,227,229,335,341,363..365,389..390,393, 554..556,615,620) /site_type="other" /note="CoA binding site [chemical binding]" /db_xref="CDD:213313" Region 224..227 (RGGR) /region_name="Coenzyme A binding. {ECO:0000250}" /experiment="experimental evidence, no additional details recorded" /note="propagated from UniProtKB/Swiss-Prot (Q9NUB1.2)" Site order(291,294..299,301..302) /site_type="other" /note="acyl-activating enzyme (AAE) consensus motif" /db_xref="CDD:213313" Site order(340..341,416..419,441..446,531,543,546,557) /site_type="other" /note="AMP binding site [chemical binding]" /db_xref="CDD:213313" Site order(340..341,416..417,444) /site_type="other" /note="acetate binding site [chemical binding]" /db_xref="CDD:213313" Site 396 K /site_type="acetylation" /experiment="experimental evidence, no additional details recorded" /note="N6-acetyllysine. {ECO:0000244|PubMed:19608861}; propagated from UniProtKB/Swiss-Prot (Q9NUB1.2)" Site 640 K /site_type="acetylation" /experiment="experimental evidence, no additional details recorded" /note="N6-acetyllysine. {ECO:0000269|PubMed:16788062}; propagated from UniProtKB/Swiss-Prot (Q9NUB1.2)" CDS 1..687 /gene="ACSS1" /gene_synonym="ACAS2L; ACECS1; AceCS2L" /coded_by="NM_001252675.1:81..2144" /note="isoform 2 precursor is encoded by transcript variant 2" /db_xref="GeneID:84532" /db_xref="HGNC:HGNC:16091" /db_xref="MIM:614355" ORIGIN 1 maartlgrgv grllgslrgl sgqparppcg vsaprraasg psgsapavaa aaaqpgsypa 61 lsaqaarepa afwgplardt lvwdtpyhtv wdcdfstgki gwflggqlnv svncldqhvr 121 kspesvaliw erdepgtevr ityrellett crlantlkrh gvhrgdrvai ympvsplava 181 amlacariga vhtvifagfs aeslagrind akckvvitfn qglrggrvve lkkivdeavk 241 hcptvqhvlv ahrtdnkvhm gdldvpleqe makedpvcap esmgsedmlf mlytsgstgm 301 pkgivhtqag yllyaalthk lvfdhqpgdi fgcvadigwi tghsyvvygp lcngatsvlf 361 estpvypnag rywetverlk inqfygapta vrlllKygda wvkkydrssl rtlgsvgepi 421 nceawewlhr vvgdsrctlv dtwwqtggic iaprpseega eilpamamrp ffgivpvlmd 481 ekgsvvegsn vsgalcisqa wpgmartiyg dhqrfvdayf kaypgyyftg dgayrteggy 541 yqitgrmddv inisghrlgt aeiedaiadh pavpesavig yphdikgeaa fafivvkdsa 601 gdsdvvvqel ksmvatkiak yavpdeilvv krlpktrsgK vmrrllrkii tseaqelgdt 661 ttledpsiia eilsvyqkck dkqaaak //
 
 
 
 
Mitä  tutkimuksia tästä geenituotteesta on saatavilla?  Huomaa SIRT3:n osuus mitokondriassa!
Related articles in PubMed
GeneRIFs: Gene References Into Functions
Kommentti: Kommentti seuraavan otsikon alla siteeraan lähdetietoa systolisesta asetyyliCoA syntetaasista.
 
 

Teknisesti syntetisoidusta aktivoidusta etikkahaposta, AcetylCoA

Ensinnäkin näyttää yritetyn syntetisoida aktivoitunutta etikkahappoa ja tästä on iso juttu netissä. Linkki tähän:
https://www.nature.com/articles/s41467-019-09095-z
Mahtava onnistunut synteesi on tehty aivan äskettäin ja artikkeli on uunituore maaliskuusta 2019:
Muta nyt otin tämän aiheen sen takia, että katson sirtuiinien osuutta  etikkahapon ja aktiivin etikkahapon sykliin. 

Article | Open | Published:
Constructing a synthetic pathway for acetyl-coenzyme A from one-carbon through enzyme design

söndag 28 april 2019

isopropyylisitraatti E384

Synonym(s)
  • Isopropyl Citrate mixture
Functional Classes
  • Antioxidant
  • Preservative
  • Sequestrant
JECFA Lookup Click here to search the FAO JECFA database for the specifications of additive(s) with INS No. 384
 Click here to search the WHO JECFA database for evaluation of additive(s) with INS No. 384
GSFA Provisions for Isopropyl citrates


Number Food Category Max Level Notes
Food Category Hierarchy 08.3.1.2 Cured (including salted) and dried non-heat treated processed comminuted meat, poultry, and game products 200 mg/kg
Food Category Hierarchy 08.2.1.2 Cured (including salted) and dried non-heat treated processed meat, poultry, and game products in whole pieces or cuts 200 mg/kg
Food Category Hierarchy 02.2.2 Fat spreads, dairy fat spreads and blended spreads 100 mg/kg
Food Category Hierarchy 08.1.2 Fresh meat, poultry, and game, comminuted 200 mg/kg
Food Category Hierarchy 02.1.3 Lard, tallow, fish oil, and other animal fats 200 mg/kg
Food Category Hierarchy 02.1.2 Vegetable oils and fats 200 mg/kg
Food Category Hierarchy 14.1.4 Water-based flavoured drinks, including "sport," "energy," or "electrolyte" drinks and particulated drinks 200 mg/kg
Note: Unless otherwise specified, food additive provisions apply to the food category indicated (e.g. Dairy), as well as to all subcategories of that category (e.g. Cheese, Ripened Cheese, etc.).

GSFA Home Food Categories Food Additives Search Functional Classes Glossary
Isopropyl citrates (384)

Propionihappo E280


GSFA Provisions for Propionic acid


Number Food Category Max Level Notes
Food Category Hierarchy 01.6.6 Whey protein cheese 3,000 mg/kg
Note: Unless otherwise specified, food additive provisions apply to the food category indicated (e.g. Dairy), as well as to all subcategories of that category (e.g. Cheese, Ripened Cheese, etc.).

GSFA Table 3 Provisions
Propionic acid is a food additive that is included in Table 3, and as such may be used in the following foods under the conditions of good manufacturing practices (GMP) as outlined in the Preamble of the Codex GSFA. Although not listed below, Propionic acid could also be used in heat-treated butter milk of food category 01.1.1 and spices of food category 12.2.1. Note that food categories listed in the Annex to Table 3 were excluded accordingly. Propionic acid is acceptable in foods conforming to the following commodity standards: CS 117-1981 CS 291-2010


Number Food Category
Food Category Hierarchy 01.1.4 Flavoured fluid milk drinks
Food Category Hierarchy 01.3 Condensed milk and analogues (plain)
Food Category Hierarchy 01.4.3 Clotted cream (plain)
Food Category Hierarchy 01.4.4 Cream analogues
Food Category Hierarchy 01.5 Milk powder and cream powder and powder analogues (plain)
Food Category Hierarchy 01.6.1 Unripened cheese
Food Category Hierarchy 01.6.2 Ripened cheese
Food Category Hierarchy 01.6.4 Processed cheese
Food Category Hierarchy 01.6.5 Cheese analogues
Food Category Hierarchy 01.7 Dairy-based desserts (e.g. pudding, fruit or flavoured yoghurt)
Food Category Hierarchy 01.8.1 Liquid whey and whey products, excluding whey cheeses
Food Category Hierarchy 02.2.2 Fat spreads, dairy fat spreads and blended spreads
Food Category Hierarchy 02.3 Fat emulsions mainly of type oil-in-water, including mixed and/or flavoured products based on fat emulsions
Food Category Hierarchy 02.4 Fat-based desserts excluding dairy-based dessert products of food category 01.7
Food Category Hierarchy 03.0 Edible ices, including sherbet and sorbet
Food Category Hierarchy 04.1.2 Processed fruit
Food Category Hierarchy 04.2.2.2 Dried vegetables (including mushrooms and fungi, roots and tubers, pulses and legumes, and aloe vera), seaweeds, and nuts and seeds
Food Category Hierarchy 04.2.2.3 Vegetables (including mushrooms and fungi, roots and tubers, pulses and legumes, and aloe vera), and seaweeds in vinegar, oil, brine, or soybean sauce
Food Category Hierarchy 04.2.2.4 Canned or bottled (pasteurized) or retort pouch vegetables (including mushrooms and fungi, roots and tubers, pulses and legumes, and aloe vera), and seaweeds
Food Category Hierarchy 04.2.2.5 Vegetable (including mushrooms and fungi, roots and tubers, pulses and legumes, and aloe vera), seaweed, and nut and seed purees and spreads (e.g., peanut butter)
Food Category Hierarchy 04.2.2.6 Vegetable (including mushrooms and fungi, roots and tubers, pulses and legumes, and aloe vera), seaweed, and nut and seed pulps and preparations (e.g. vegetable desserts and sauces, candied vegetables) other than food category 04.2.2.5
Food Category Hierarchy 04.2.2.8 Cooked or fried vegetables (including mushrooms and fungi, roots and tubers, pulses and legumes, and aloe vera), and seaweeds
Food Category Hierarchy 05.0 Confectionery
Food Category Hierarchy 06.3 Breakfast cereals, including rolled oats
Food Category Hierarchy 06.4.3 Pre-cooked pastas and noodles and like products
Food Category Hierarchy 06.5 Cereal and starch based desserts (e.g. rice pudding, tapioca pudding)
Food Category Hierarchy 06.6 Batters (e.g. for breading or batters for fish or poultry)
Food Category Hierarchy 06.7 Pre-cooked or processed rice products, including rice cakes (Oriental type only)
Food Category Hierarchy 06.8 Soybean products (excluding soybean-based seasonings and condiments of food category 12.9)
Food Category Hierarchy 07.0 Bakery wares
Food Category Hierarchy 08.2 Processed meat, poultry, and game products in whole pieces or cuts
Food Category Hierarchy 08.3 Processed comminuted meat, poultry, and game products
Food Category Hierarchy 08.4 Edible casings (e.g. sausage casings)
Food Category Hierarchy 09.3 Semi-preserved fish and fish products, including mollusks, crustaceans, and echinoderms
Food Category Hierarchy 09.4 Fully preserved, including canned or fermented fish and fish products, including mollusks, crustaceans, and echinoderms
Food Category Hierarchy 10.2.3 Dried and/or heat coagulated egg products
Food Category Hierarchy 10.3 Preserved eggs, including alkaline, salted, and canned eggs
Food Category Hierarchy 10.4 Egg-based desserts (e.g. custard)
Food Category Hierarchy 11.6 Table-top sweeteners, including those containing high-intensity sweeteners
Food Category Hierarchy 12.2.2 Seasonings and condiments
Food Category Hierarchy 12.3 Vinegars
Food Category Hierarchy 12.4 Mustards
Food Category Hierarchy 12.5 Soups and broths
Food Category Hierarchy 12.6 Sauces and like products
Food Category Hierarchy 12.7 Salads (e.g. macaroni salad, potato salad) and sandwich spreads excluding cocoa- and nut-based spreads of food categories 04.2.2.5 and 05.1.3
Food Category Hierarchy 12.8 Yeast and like products
Food Category Hierarchy 12.9 Soybean-based seasonings and condiments
Food Category Hierarchy 12.10 Protein products other than from soybeans
Food Category Hierarchy 13.3 Dietetic foods intended for special medical purposes (excluding products of food category 13.1)
Food Category Hierarchy 13.4 Dietetic formulae for slimming purposes and weight reduction
Food Category Hierarchy 13.5 Dietetic foods (e.g. supplementary foods for dietary use) excluding products of food categories 13.1 - 13.4 and 13.6
Food Category Hierarchy 13.6 Food supplements
Food Category Hierarchy 14.1.4 Water-based flavoured drinks, including "sport," "energy," or "electrolyte" drinks and particulated drinks
Food Category Hierarchy 14.2.1 Beer and malt beverages
Food Category Hierarchy 14.2.2 Cider and perry
Food Category Hierarchy 14.2.4 Wines (other than grape)
Food Category Hierarchy 14.2.5 Mead
Food Category Hierarchy 14.2.6 Distilled spirituous beverages containing more than 15% alcohol
Food Category Hierarchy 14.2.7 Aromatized alcoholic beverages (e.g. beer, wine and spirituous cooler-type beverages, low alcoholic refreshers)
Food Category Hierarchy 15.0 Ready-to-eat savouries
Food Category Hierarchy 16.0 Prepared foods
Note: Unless otherwise specified, food additive provisions apply to the food category indicated (e.g. Dairy), as well as to all subcategories of that category (e.g. Cheese, Ripened Cheese, etc.).
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