Escherichia coli K-12 substr. MG1655 Enzyme: maltose acetyltransferase

Gene: maa Accession Numbers: G58 (EcoCyc), b0459, ECK0453

Synonyms: ylaD

Regulation Summary Diagram: ?

Regulation summary diagram for maa

Subunit composition of maltose acetyltransferase = [Maa]2

Maltose acetyltransferase has broad substrate specificity, and is capable of acetylating many sugars. The enzyme is not part of the maltose system. Its specific physiological role is not known but it is thought that the enzyme prevents the accumulation of free sugars to high levels through acetylation, playing a detoxifying role in the cell. Acetylmaltose is excreted into the culture medium in malB+ malQ strains which accumulate maltose but cannot metabolise it [Brand91, Freundlieb82, Boos81].

Locations: cytosol

Map Position: [478,591 <- 479,142] (10.32 centisomes, 37°)
Length: 552 bp / 183 aa

Molecular Weight of Polypeptide: 20.096 kD (from nucleotide sequence), 20.0 kD (experimental) [Brand91 ]

Molecular Weight of Multimer: 40.0 kD (experimental) [Soler08]

Unification Links: ASAP:ABE-0001591 , DIP:DIP-10140N , EchoBASE:EB3990 , EcoGene:EG14239 , EcoliWiki:b0459 , ModBase:P77791 , OU-Microarray:b0459 , PortEco:maa , PR:PRO_000023143 , Protein Model Portal:P77791 , RefSeq:NP_414992 , RegulonDB:G58 , SMR:P77791 , String:511145.b0459 , UniProt:P77791

Relationship Links: InterPro:IN-FAMILY:IPR011004 , InterPro:IN-FAMILY:IPR018357 , InterPro:IN-FAMILY:IPR024688 , PDB:Structure:1OCX , Pfam:IN-FAMILY:PF12464 , Prosite:IN-FAMILY:PS00101

In Paralogous Gene Group: 11 (13 members)

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0008152 - metabolic process Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01, GOA01a, Brand91]
Molecular Function: GO:0008925 - maltose O-acetyltransferase activity Inferred from experiment Inferred by computational analysis [GOA01, Brand91]
GO:0016407 - acetyltransferase activity Inferred by computational analysis [GOA01a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: cell processes adaptations other (mechanical, nutritional, oxidative stress)

Essentiality data for maa knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Enzymatic reaction of: maltose acetyltransferase

Synonyms: maltose transacetylase

EC Number:

maltose + acetyl-CoA <=> acetylmaltose + coenzyme A

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

This reaction is reversible.

Alternative Substrates for maltose: β-D-glucopyranose , D-mannose , β-D-galactose , D-fructose

Inhibitors (Competitive): coenzyme A [Comment 5]

Primary Physiological Regulators of Enzyme Activity: coenzyme A

Kinetic Parameters:

Km (μM)
[Brand91, BRENDA14]

pH(opt): 7.8 [BRENDA14, Lo03]

Sequence Features

Protein sequence of Maa with features indicated

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
[Wilkins98, UniProt11]
UniProt: Removed.
Chain 2 -> 183
UniProt: Maltose O-acetyltransferase;

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


4/2/1999 (pkarp) Merged genes G6254/b0459 and G58/maa
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Boos81: Boos W, Ferenci T, Shuman HA (1981). "Formation and excretion of acetylmaltose after accumulation of maltose in Escherichia coli." J Bacteriol 1981;146(2);725-32. PMID: 7012137

Brand91: Brand B, Boos W (1991). "Maltose transacetylase of Escherichia coli. Mapping and cloning of its structural, gene, mac, and characterization of the enzyme as a dimer of identical polypeptides with a molecular weight of 20,000." J Biol Chem 1991;266(21);14113-8. PMID: 1856235

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014."

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Freundlieb82: Freundlieb S, Boos W (1982). "Maltose transacetylase of Escherichia coli: a preliminary report." Ann Microbiol (Paris) 1982;133A(1);181-9. PMID: 7041741

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Lo03: Lo Leggio L, Dal Degan F, Poulsen P, Andersen SM, Larsen S (2003). "The structure and specificity of Escherichia coli maltose acetyltransferase give new insight into the LacA family of acyltransferases." Biochemistry 42(18);5225-35. PMID: 12731863

Soler08: Soler JK, Okkes I, Wood M, Lamberts H (2008). "The coming of age of ICPC: celebrating the 21st birthday of the International Classification of Primary Care." Fam Pract 25(4);312-7. PMID: 18562335

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Wilkins98: Wilkins MR, Gasteiger E, Tonella L, Ou K, Tyler M, Sanchez JC, Gooley AA, Walsh BJ, Bairoch A, Appel RD, Williams KL, Hochstrasser DF (1998). "Protein identification with N and C-terminal sequence tags in proteome projects." J Mol Biol 278(3);599-608. PMID: 9600841

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Wed Oct 7, 2015, biocyc12.