Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
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MetaCyc Reaction: 2.7.1.162

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 2.7.1.162

Enzymes and Genes:
N-acetylhexosamine kinase Inferred from experiment : lnpB ( Bifidobacterium longum )

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Instance reaction:
ATP + N-acetyl-α-D-galactosamine = ADP + N-acetyl-α-D-galactosamine 1-phosphate + H+ (2.7.1.157)

Enzyme Commission Primary Name: N-acetylhexosamine 1-kinase

Enzyme Commission Synonyms: NahK, LnpB, N-acetylgalactosamine/N-acetylglucosamine 1-kinase

Standard Gibbs Free Energy (ΔrG in kcal/mol): -14.815857 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
Differs from EC 2.7.1.157, N-acetylgalactosamine kinase, as it can phosphorylate both N-acetyl-α-D-galactosamine and N-acetyl-β-D-glucosamine at similar rates. Also has some activity with N-acetyl-β-D-mannosamine, D-talose and D-mannose as substrate. ATP can be replaced by GTP or ITP but with decreased enzyme activity. Requires a divalent cation, with Mg2+ resulting in by far the greatest stimulation of enzyme activity [Nishimoto07].

Gene-Reaction Schematic: ?

Instance reaction of [an N-acetyl-D-hexosamine + ATP = an N-acetyl-α-D-hexosamine 1-phosphate + ADP + H+] (2.7.1.162):
i1: ATP + N-acetyl-α-D-galactosamine = ADP + N-acetyl-α-D-galactosamine 1-phosphate + H+ (2.7.1.157)

Unification Links: Rhea:25428

Relationship Links: BRENDA:EC:2.7.1.162 , ENZYME:EC:2.7.1.162 , IUBMB-ExplorEnz:EC:2.7.1.162


References

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Nishimoto07: Nishimoto M, Kitaoka M (2007). "Identification of N-acetylhexosamine 1-kinase in the complete lacto-N-biose I/galacto-N-biose metabolic pathway in Bifidobacterium longum." Appl Environ Microbiol 73(20);6444-9. PMID: 17720833


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Mon Dec 22, 2014, biocyc14.